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It might be helpful to include some mention of the T and R states in this section. It does address the change in conformation, but specificity is always preferred. Dykeszr ( talk) 14:37, 6 April 2017 (UTC)Dykeszr
The graphic shows the change from T to R state, which is really informative so I believe that inclusion of the specific states and some information on them would benefit the page AshleyJennings ( talk) 18:13, 14 October 2020 (UTC)
is it better to have structure and synthesis together? The edit about chemical formula of Hb is not accurate. Does it refer to HbA, HbA2, HbF which have varying numbers of amino acids? " Hemoglobin is chemically represented by (C2952H4664N812O832S8Fe4). "
As I see it, the empirical formula C738H1166N812O203S2Fe is not correct. This because it doesn't add up if you multiply it by four (which I assume the original formula was divided with). Yfé ( talk) 09:37, 1 December 2008 (UTC)
How long does it take for hemoglobin to decay if blood falls out of a slaughtered animal onto the ground (or someplace not in the animal)? Chiss Boy 12:34, 4 March 2007 (UTC)
I read some time ago that while in "higher" animals including humans, 2 strands of alpha-hemoglobin combine with 2 strands of beta-hemoglobin, in "lesser" animals, the hemoglobin consists only of 2 alpha-strands (enclosing, as usual, an iron atom). Unfortunately, I had no luck finding more info on the Internet - could somebody who knows about this please elaborate? Aragorn2 11:50, 23 Oct 2004 (UTC)
If you go "low" enough, hemoglobin acts on nitrous oxide rather than oxygen [1]. A little "higher" and animals have large molecular weight hemoglobins that are carried in the plasma. Move on up to birds and mammals, and there's small molecular weight hemoglobins that are packaged in red blood cells [2]. The respiratory protein of "lower" animals certainly isn't always simpler (snail hemocyanin, for example, has 10 subunits). I don't know of any animals that have only two alpha-strands as a functional hemoglobin, and alpha-beta dimers are ineffective oxygen carriers, so something's been lost since your read it, or the missing info is in a veterinary source somewhere. - Nunh-huh 14:08, 23 Oct 2004 (UTC)
Thanks for the links. I had read about the worm before, but from this text, it's not obvious whether the worm has dimer or tetramer (or even monomer?) hemoglobin. After another Google search, I found this:
and a possible scenario for hemoglobin evolution on this page:
So the lamprey has alpha-alpha-dimer hemoglobin which splits apart when oxygenated, which is what I was referring to.
Got it now.. looks like:
That was a very interesting question! we ought to put a chart or a synopsis in the article. - Nunh-huh 03:52, 24 Oct 2004 (UTC)
There are variety of hemoglobin predecessors, many of which have different names. Such as Erythrocruorin in worms and myoglobin which is a monomer and has no arrogating ability. Erythrocruorin should get an article for it self, I can easily scrounge up enough information and generate image of the protein from pubmed, but I lack the time.-- BerserkerBen 22:58, 31 Jan 2005 (UTC)
I don't know much about the chemistry of hemoglobin and the like, but a section detailing how and why hemoglobin levels are measured in humans. A table or something illustrating the distribution and ideal hemoglobin level would also be great. My doctor just called me and all he said was "14,7" and I have absolutly no clue what that means. Google will answer me in minutes, but still, I was hoping Wikipedia would have it. -- Crucible Guardian 6 July 2005 01:29 (UTC)
Sometime in the past I read that in humans, oxygen transport decreases by 1% per year after the age of 20, which I can believe, being now 65. Is there information on the aging process and oxygen transport that could be summarized in a short paragraph? — Preceding unsigned comment added by 71.141.160.19 ( talk) 04:59, 2005 December 2 (UTC)
This article goes back and forth between hemoglobin and haemoglobin. Pick one and stick with it, but mention both in the first sentence. I believe the hemoglobin spelling is more universal throughout medical literature, but I don't know about common usage outside the US. Hichris 17:39, 16 December 2005 (UTC)
Yeah we should really be using haemoglobin. —Preceding unsigned comment added by 194.81.199.59 ( talk) 16:44, 11 February 2008 (UTC)
Hemoglobin is the spelling far more commonly used in scientific literature. Searching Medline turns up ~76,000 hits for "hemoglobin" and under 20,000 for "haemoglobin." —Preceding unsigned comment added by 128.237.250.128 ( talk) 20:32, 24 April 2008 (UTC)
The Lancet gives 18 results for hemoglobin, and 1596 results for haemoglobin... —Preceding unsigned comment added by 86.150.188.15 ( talk) 14:35, 23 January 2011 (UTC)
As the World Health Organisation uses the spelling "haemoglobin" would it not be more correct to use that spelling? —Preceding unsigned comment added by 78.144.149.123 ( talk) 21:33, 16 February 2011 (UTC)
I tried a redirect but some automated process is not letting me to add the content to the Haemoglobin part. Some one fix it! 61.3.151.103 ( talk) 09:52, 29 July 2018 (UTC)
Anyone think this artilce shoukld be nominated as a feature article? If not why?-- BerserkerBen 07:31, 31 December 2005 (UTC)
I can think of some points. Firstly, the spelling is inconsistent (BE/AE). There is no history section; we don't learn who discovered it, when it was first sentenced, linked and cloned, why Linus Pauling won the Nobel Prize in relation to it, why the Bohr effect is called like that, etc etc. In short, more context. Classic references are very useful. JFW | T@lk 21:28, 17 January 2006 (UTC)
"Hemoglobin or haemoglobin (frequently abbreviated as Hb or Hgb) is the iron-containing oxygen-transport metalloprotein in the red cells of the blood in mammals and other animals; in mammals the protein makes up about 97% of the red cell’s dry content, and around 35%, including water."
35% .. ??
Jdruiter 23:32, 28 January 2007 (UTC)
I was in the ER two times yesterday with my sister for nausea.Her hemoglobin was 7.9.today she still has a bad lingering headache. Could this headache be caused from her low hemoglobin? She has been sick for years. She's has really bad migraines, has had her gallbladder and half her intestines taken out,and she can't digest her food which makes her throw up.she's had to have a blood transfusion 5 months ago, because her hemoglobin was 6.1.Can anyone answer my question about if low hemoglobin can cause her to have this lingering headache?(she only weighs 80 lbs and is 56 yrs.old.)(she said this headache is not like her migraines.)
Thank you, Sincerley Judy Vasilis
I have undone a recent addition of a second image to show the R to T transformation. [4] The reasoning is that, although the second image does show all 4 chains and you could argue that two images are better than one, the text was being crushed up along the left hand side (as the second image is so big) and the sigmoid curve image (which is already some distance from the text referring to it) was being pushed further down the page. If someone who is better at image placement than I am can resolve these difficulties I would have no problem with the 2 images. Thanks. Mmoneypenny 21:55, 28 April 2007 (UTC)
I'll do my best to make two pics of hemoglobin at 180px come out without shoving the sigmoid curve too far down. But we really need two pics of hemoglobin motion at least as much as the sigmoid curve. S B H arris 22:09, 28 April 2007 (UTC)
I haven't found a way to keep text out of a section that you only want to put illustration boxes in, no matter the size. I finally put in enough equalsign spacer to keep text out of there no matter what the illustration size is. What do you think of the look now?
The main reason I'm trying to keep the old illustration in is not because I made it or had anything to do with it. But it shows the motion of the porphyrin ring-- how it moves to react with the O2 and tugs on its peptide chain by doing so, far better than the other. I can almost see all the details of how the molecule works here, and would far rather remove the latest version, if I had to pick one. S B H arris 05:38, 30 April 2007 (UTC)
(cough)I was the one that made taht animation if you need my help or anthing? (cough) -- BerserkerBen 23:38, 30 April 2007 (UTC)
The animated gif is very nice for demonstrating not only that the chains move relative to each other, but also that while internal conformation changes occur in the alpha chains, the beta chains move pretty much as rigid bodies. Unfortunately the helix definitions in the beta chain on the right have been made differently in the two states, so one helix dissolves completely and another loses one turn, in going from deoxy to oxy form. The picture should be remade with the same helix definitions in oxy as in deoxy. Eaberry ( talk) 15:18, 12 April 2011 (UTC)
I have been studying hemoglobin's structure and many biochemistry textbooks are contradictory on whether identical (alpha or beta) subunits are adjacent or diagonal. The first image of this article has them labeled diagonally whereas this image has them labeled adjacent. Frustrated, I visited what I believe is the most authoritative site: the PDB (Protein Data Bank) which catalogs the x-ray crystal or NMR structures determined by research groups and found that the correct labeling is diagonal (as in the top diagram of this article). Thought you might like to know this. Thanks. 126lys ( talk) 19:09, 4 January 2011 (UTC)
The section about the oxidation state of iron in oxyhaemoglobin is wrong. It is now known that it is low-spin Fe(II). See Greenwood and Earshaw, Chemistry of the Elements 2nd edition, pp 1099-1100. The key point is that in deoxy-Hb the high-spin Fe(II) is too large to enter the plane of the porphirin ring (Figure 25.7) but when oxygen binds the low-spin Fe(II) enters the plane as it is small enough. The paramagnetism of O2 is destroyed because the Fe-O2 angle is 120o, so the pi-star orbitals are no longer doubly degenerate.
I'm not a biochemist, so I hesitate to edit the article myself. Petergans 09:56, 11 May 2007 (UTC)
-SBHarris, do you have reference for that? —Preceding
unsigned comment added by
216.80.44.45 (
talk)
02:06, 24 October 2008 (UTC)
Can we get a primary reference for the claim that IR frequencies change with the state of O2? For example is this Raman data or IR data? IR is usually not ideal for measuring absorption of diatomic molecules (though this may not be a problem for O2 coordinated with the hemoglobin). Jesse Greener ( talk) 19:40, 2 April 2010 (UTC)
Is it called hemoglobin or haemoglobin. The title says hemoglobin but in the opening line of the article it says haemoglobin. Which one should be changed? Ziphon 02:47, 29 May 2007 (UTC)
The original article was written in British English, and according to wikipedia rules, any form of english that is widely accepted is acceptable, so long that this was the original form the article took. Applying this, given the original article (tracking history back as far as i can) has the spelling 'haemoglobin', I move for this to be reinstated. 86.7.204.43 ( talk) 21:30, 30 August 2008 (UTC)
I come from more of a genetics background and knew hemoglobin in the context of the alpha globin locus, the beta globin locus and locus control region, the genes, etc. It took me forever to get my bearings here because "variants" refer to different combinations of protein subunits, not different protein subunits themselves. I now realize that α,β,etc. are the protein subunits, but I don't think this was explained very well and the protein subunits themselves definitely aren't talked about much. For now I'll just add links under "See also" to the genes, since I'm not sure on a good consistent nomenclature for the article. Forluvoft 06:52, 3 November 2007 (UTC)
The genetics of haemoglobin is quite complex and changes with the age of the embryo and child. None of the complexity is shown here. Please see the article on Fetal haemoglobin; http://en.wikipedia.org/wiki/Fetal_hemoglobin for a start. The genetics are also very interesting as the gene is really more of a region than a locus. Most of the sequence is coded forward but some is coded in reverse direction. Sequences are moved around as transcribed into mRNA and then other sequences are moved and deleted in the protein assembly. This synthesis is missing. 198.103.184.76 ( talk) —Preceding undated comment added 15:39, 11 March 2013 (UTC)
The "role in disease" section lists several diseases of "too little" or "broken" hemoglobin. What is it when you have too much hemoglobin? Polycythemia? Something else? WhatamIdoing ( talk) 03:55, 22 August 2008 (UTC)
I do not know much about the chemistry of hemoglobin and the like, but a section detailing how and why hemoglobin levels are measured in humans. A table or something illustrating the distribution and ideal hemoglobin level would also be great. My doctor just called me and all he said was 7 and I have absolutly no clue what that means. Google will answer me in minutes, but still, I was hoping Wikipedia would have it. --Crucible Guardian 6 July 2005 01:29 (UTC) —Preceding unsigned comment added by Ohiohealthquiz ( talk • contribs)
I don't know about this edit. If we've got a source that says 1851, then why are we replacing it with one that asserts a 1940 discovery? WhatamIdoing ( talk) 20:11, 8 January 2009 (UTC)
From the paragraph headed Research History:
Not a claim of discovery, but a fairly strong implication that someone else had already discovered hæmoglobin; granted, Engelhard did not use that term but instead called it vera materia sanguini purpureum colorem.
I found this on an American Chemical Society webpage ( https://www.acs.org/content/acs/en/molecule-of-the-week/archive/h/hemoglobin.html):
Here are some significant events in the history of hemoglobin discovery:
- 1825: J. F. Engelhard shows that the Fe/protein ratio is the same in several species’ hemoglobin.
- 1840: F. L. Hünefeld discovers that hemoglobin transports oxygen.
I think that makes "protein" a likely typo for "property of" in the bit about Hünefeld, but I do not have access to the primary sources. Regardless, for Engelhard to have come up with such a close (and, at the time, astonishing) estimate for the molecular mass of hæmoglobin deserves a much wider currency.
I'm going to make the edit and see what turns up. Moletrouser ( talk) 10:21, 23 September 2018 (UTC)
This is a very interesting article, with great information and graphics. However, I must comment that this page seems to require too much prior knowledge of biochemistry or medicine from the general reader, the presumed audience/user. For instance, why the presumption that the reader knows what an "erythrocyte" is? It would be arrogant to say, "Well, they can just look it up." That is poor editing if the intended audience is not limited to those with a chemical or biological major in college or medical school training. Why not at least define as "red blood cells"? Also, the inconsistent spelling of hemoglobin in the very heavy section "Presence in nonerythroid cells" is distracting and possibly confusing, if one didn`t know that that was all it was. Again, this article is impressive, esp. as it is "Scot-free"! (non-PC comment, LOL) Jack B108 ( talk) 02:03, 15 January 2010 (UTC)
If you find places where you find the techical level unevenness unusually bad, I suggest you fix it by adding introductory explanatory material to get from the level you feel comfortable at, to that of the present text. If doing so increases the length of this article so much that further spin-offs become necessary, that's fine! It will then trigger the WP:SS mechanism. So this is a natural mechanism of growth, and a self-regulating one when it comes to technical level. It's just that this sort of evolution occurs with less gradualism and uniformity than many people who are used to "non-grown" encyclopedias are comfortable with. S B H arris 02:57, 15 January 2010 (UTC)
This section gives a good account of the historical facts, but the conclusion is now known to be wrong - see Greenwood, Norman N.; Earnshaw, Alan (1997). Chemistry of the Elements (2nd ed.). Butterworth-Heinemann. ISBN 978-0-08-037941-8. p. 1099. Hb-O2 is a complex of low-spin iron(II) with the oxygen molecule. The angle Fe-O-O is not 180°. The non-linearity destroys the degeneracy of the π* orbitals and so the electrons which have paralell spins in the oxygen molecule can pair up in the complex at a lower energy cost than is required to form the singlet state in the isolated oxygen molecule. This section therefore need more attention than I feel qualified to give, as I'm not expert in biochemistry. Petergans ( talk) 14:12, 17 March 2010 (UTC)
Conversion between g/dl is given differently in different sections (quotes A and B below).
A) Each subunit has a molecular weight of about 17,000 daltons, for a total molecular weight of the tetramer of about 68,000 daltons (64,458 g/mol)[24]. Thus, 1 g/dL = 0.1551 mmol/L.
B) Hemoglobin concentration measurement is among the most commonly performed blood tests, usually as part of a complete blood count. For example it is typically tested before or after blood donation. Results are reported in g/L, g/dL or mol/L. 1 g/dL equals about 0.6206 mmol/L
The former is intuitively right as it uses to the full weight of tetrameric haemoglobin, but it is the latter (that gives the concentration of heme-groups, 1 per subunit of approximately 16000) that is consictent with my ADVIA outputs. Can anyone give me a reason for this discrepancy?
The article talks about the fact that glucose can bond to haemoglobin, and the diagnostic use of this, but doesn't mention a physiological role. Is there one? Why is haemoglobin able to combine with glucose? It would certainly help the article to either explain one, or to say that none is known, as most readers are bound to wonder about this. 144.32.126.16 ( talk) 10:03, 24 September 2010 (UTC)
It is not clear whether it is easier or more difficult for the fourth oxygen molecule to bind (as far as I know, it is more difficult) and the paragraph implies otherwise.
59.182.159.57 ( talk) 03:43, 25 October 2010 (UTC)
Based on a quick check of an online dictionary, the word "heme" was first used in 1925, well after the use of "hemoglobin". I would "guess" that the word is based on "hemo-" (blood) and "globin" (roundish protein) and was called that before heme was discovered, but I don't have a reference source to verify this. Anyone else have a specific reference for this? -- Kris ( talk) 17:18, 30 December 2011 (UTC)
Section: Oxygen saturation Narrative: "In general, hemoglobin can be saturated with oxygen molecules (oxyhemoglobin), or desaturated with oxygen molecules (deoxyhemoglobin)"
The phrase "desaturated with oxygen molecules" is difficult to parse. Does this simply mean "lacking in oxygen molecules", or does it mean "can be desaturated, by using oxygen molecules"? Pretty sure the former, but this is a very strange way to say so.
Also, is there no intermediate state of partially filled with oxygen molecules? — Preceding unsigned comment added by Gwideman ( talk • contribs) 18:35, 1 April 2013 (UTC)
The picture of heme shows the binding of CO2, but in many works is shown, that it is more probable of binding it to the amino ends of each four chains. Also the name carbamino is telling about the reaction CO2(carb) + -NH2(amino) = -NHCOOH more than Fe + CO2 = FeCO2+ or what it is? — Preceding unsigned comment added by MarekMatejak ( talk • contribs) 23:19, 26 June 2013 (UTC)
The comment(s) below were originally left at Talk:Hemoglobin/Comments, and are posted here for posterity. Following several discussions in past years, these subpages are now deprecated. The comments may be irrelevant or outdated; if so, please feel free to remove this section.
Very nicely done article: should need relatively little work to advance it to FA status. – Clockwork Soul |
Last edited at 21:06, 23 October 2006 (UTC). Substituted at 17:37, 29 April 2016 (UTC)
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The result of the move request was: no consensus to move the page to the proposed title at this time, per the discussion below. Dekimasu よ! 06:19, 5 August 2018 (UTC)
Hemoglobin → Haemoglobin – The preferred title has been discussed informally before, but it seems like it is time for a formal move discussion after a recent cut'n'paste move attempt. Haemoglobin is the traditional spelling, but hemoglobin is arguably now more common. See discussion above. Lithopsian ( talk) 11:30, 29 July 2018 (UTC)
Would anyone be opposed to me cleaning up and shortening the section on the oxidation state? It's all good information, but it's something of a rabbit hole that is probably not of interest (or accessible) to a general audience. I think it could all be summarized in a paragraph, pointing out the conflicting models and stating that there is disagreement about the matter. If there is general consensus to keep it the way it is, I'll shut up. WeirdNAnnoyed ( talk) 03:04, 18 April 2023 (UTC)
From this article:
From the article blood:
1060 kg/m3 = 106g per 100 mL
35% of 106g = 37g, well outside stated the range 12 to 20 grams
Sorry, I overlooked that 35% is for a blood cell, not blood as a whole.
Another thing, isn't it weird to give the density of blood in kg/m3? Wouldn't g/cm3 be more normal? 2A00:23C8:7B09:FA01:2165:E410:E554:7951 ( talk) 18:09, 25 February 2024 (UTC)
This
level-4 vital article is rated B-class on Wikipedia's
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This article was the subject of a Wiki Education Foundation-supported course assignment, between 6 October 2020 and 16 December 2020. Further details are available on the course page. Peer reviewers: AshleyJennings.
Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT ( talk) 22:17, 17 January 2022 (UTC)
This article was the subject of a Wiki Education Foundation-supported course assignment, between 12 August 2020 and 25 November 2020. Further details are available on the course page. Student editor(s): JoyousMuse.
Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT ( talk) 23:19, 16 January 2022 (UTC)
It might be helpful to include some mention of the T and R states in this section. It does address the change in conformation, but specificity is always preferred. Dykeszr ( talk) 14:37, 6 April 2017 (UTC)Dykeszr
The graphic shows the change from T to R state, which is really informative so I believe that inclusion of the specific states and some information on them would benefit the page AshleyJennings ( talk) 18:13, 14 October 2020 (UTC)
is it better to have structure and synthesis together? The edit about chemical formula of Hb is not accurate. Does it refer to HbA, HbA2, HbF which have varying numbers of amino acids? " Hemoglobin is chemically represented by (C2952H4664N812O832S8Fe4). "
As I see it, the empirical formula C738H1166N812O203S2Fe is not correct. This because it doesn't add up if you multiply it by four (which I assume the original formula was divided with). Yfé ( talk) 09:37, 1 December 2008 (UTC)
How long does it take for hemoglobin to decay if blood falls out of a slaughtered animal onto the ground (or someplace not in the animal)? Chiss Boy 12:34, 4 March 2007 (UTC)
I read some time ago that while in "higher" animals including humans, 2 strands of alpha-hemoglobin combine with 2 strands of beta-hemoglobin, in "lesser" animals, the hemoglobin consists only of 2 alpha-strands (enclosing, as usual, an iron atom). Unfortunately, I had no luck finding more info on the Internet - could somebody who knows about this please elaborate? Aragorn2 11:50, 23 Oct 2004 (UTC)
If you go "low" enough, hemoglobin acts on nitrous oxide rather than oxygen [1]. A little "higher" and animals have large molecular weight hemoglobins that are carried in the plasma. Move on up to birds and mammals, and there's small molecular weight hemoglobins that are packaged in red blood cells [2]. The respiratory protein of "lower" animals certainly isn't always simpler (snail hemocyanin, for example, has 10 subunits). I don't know of any animals that have only two alpha-strands as a functional hemoglobin, and alpha-beta dimers are ineffective oxygen carriers, so something's been lost since your read it, or the missing info is in a veterinary source somewhere. - Nunh-huh 14:08, 23 Oct 2004 (UTC)
Thanks for the links. I had read about the worm before, but from this text, it's not obvious whether the worm has dimer or tetramer (or even monomer?) hemoglobin. After another Google search, I found this:
and a possible scenario for hemoglobin evolution on this page:
So the lamprey has alpha-alpha-dimer hemoglobin which splits apart when oxygenated, which is what I was referring to.
Got it now.. looks like:
That was a very interesting question! we ought to put a chart or a synopsis in the article. - Nunh-huh 03:52, 24 Oct 2004 (UTC)
There are variety of hemoglobin predecessors, many of which have different names. Such as Erythrocruorin in worms and myoglobin which is a monomer and has no arrogating ability. Erythrocruorin should get an article for it self, I can easily scrounge up enough information and generate image of the protein from pubmed, but I lack the time.-- BerserkerBen 22:58, 31 Jan 2005 (UTC)
I don't know much about the chemistry of hemoglobin and the like, but a section detailing how and why hemoglobin levels are measured in humans. A table or something illustrating the distribution and ideal hemoglobin level would also be great. My doctor just called me and all he said was "14,7" and I have absolutly no clue what that means. Google will answer me in minutes, but still, I was hoping Wikipedia would have it. -- Crucible Guardian 6 July 2005 01:29 (UTC)
Sometime in the past I read that in humans, oxygen transport decreases by 1% per year after the age of 20, which I can believe, being now 65. Is there information on the aging process and oxygen transport that could be summarized in a short paragraph? — Preceding unsigned comment added by 71.141.160.19 ( talk) 04:59, 2005 December 2 (UTC)
This article goes back and forth between hemoglobin and haemoglobin. Pick one and stick with it, but mention both in the first sentence. I believe the hemoglobin spelling is more universal throughout medical literature, but I don't know about common usage outside the US. Hichris 17:39, 16 December 2005 (UTC)
Yeah we should really be using haemoglobin. —Preceding unsigned comment added by 194.81.199.59 ( talk) 16:44, 11 February 2008 (UTC)
Hemoglobin is the spelling far more commonly used in scientific literature. Searching Medline turns up ~76,000 hits for "hemoglobin" and under 20,000 for "haemoglobin." —Preceding unsigned comment added by 128.237.250.128 ( talk) 20:32, 24 April 2008 (UTC)
The Lancet gives 18 results for hemoglobin, and 1596 results for haemoglobin... —Preceding unsigned comment added by 86.150.188.15 ( talk) 14:35, 23 January 2011 (UTC)
As the World Health Organisation uses the spelling "haemoglobin" would it not be more correct to use that spelling? —Preceding unsigned comment added by 78.144.149.123 ( talk) 21:33, 16 February 2011 (UTC)
I tried a redirect but some automated process is not letting me to add the content to the Haemoglobin part. Some one fix it! 61.3.151.103 ( talk) 09:52, 29 July 2018 (UTC)
Anyone think this artilce shoukld be nominated as a feature article? If not why?-- BerserkerBen 07:31, 31 December 2005 (UTC)
I can think of some points. Firstly, the spelling is inconsistent (BE/AE). There is no history section; we don't learn who discovered it, when it was first sentenced, linked and cloned, why Linus Pauling won the Nobel Prize in relation to it, why the Bohr effect is called like that, etc etc. In short, more context. Classic references are very useful. JFW | T@lk 21:28, 17 January 2006 (UTC)
"Hemoglobin or haemoglobin (frequently abbreviated as Hb or Hgb) is the iron-containing oxygen-transport metalloprotein in the red cells of the blood in mammals and other animals; in mammals the protein makes up about 97% of the red cell’s dry content, and around 35%, including water."
35% .. ??
Jdruiter 23:32, 28 January 2007 (UTC)
I was in the ER two times yesterday with my sister for nausea.Her hemoglobin was 7.9.today she still has a bad lingering headache. Could this headache be caused from her low hemoglobin? She has been sick for years. She's has really bad migraines, has had her gallbladder and half her intestines taken out,and she can't digest her food which makes her throw up.she's had to have a blood transfusion 5 months ago, because her hemoglobin was 6.1.Can anyone answer my question about if low hemoglobin can cause her to have this lingering headache?(she only weighs 80 lbs and is 56 yrs.old.)(she said this headache is not like her migraines.)
Thank you, Sincerley Judy Vasilis
I have undone a recent addition of a second image to show the R to T transformation. [4] The reasoning is that, although the second image does show all 4 chains and you could argue that two images are better than one, the text was being crushed up along the left hand side (as the second image is so big) and the sigmoid curve image (which is already some distance from the text referring to it) was being pushed further down the page. If someone who is better at image placement than I am can resolve these difficulties I would have no problem with the 2 images. Thanks. Mmoneypenny 21:55, 28 April 2007 (UTC)
I'll do my best to make two pics of hemoglobin at 180px come out without shoving the sigmoid curve too far down. But we really need two pics of hemoglobin motion at least as much as the sigmoid curve. S B H arris 22:09, 28 April 2007 (UTC)
I haven't found a way to keep text out of a section that you only want to put illustration boxes in, no matter the size. I finally put in enough equalsign spacer to keep text out of there no matter what the illustration size is. What do you think of the look now?
The main reason I'm trying to keep the old illustration in is not because I made it or had anything to do with it. But it shows the motion of the porphyrin ring-- how it moves to react with the O2 and tugs on its peptide chain by doing so, far better than the other. I can almost see all the details of how the molecule works here, and would far rather remove the latest version, if I had to pick one. S B H arris 05:38, 30 April 2007 (UTC)
(cough)I was the one that made taht animation if you need my help or anthing? (cough) -- BerserkerBen 23:38, 30 April 2007 (UTC)
The animated gif is very nice for demonstrating not only that the chains move relative to each other, but also that while internal conformation changes occur in the alpha chains, the beta chains move pretty much as rigid bodies. Unfortunately the helix definitions in the beta chain on the right have been made differently in the two states, so one helix dissolves completely and another loses one turn, in going from deoxy to oxy form. The picture should be remade with the same helix definitions in oxy as in deoxy. Eaberry ( talk) 15:18, 12 April 2011 (UTC)
I have been studying hemoglobin's structure and many biochemistry textbooks are contradictory on whether identical (alpha or beta) subunits are adjacent or diagonal. The first image of this article has them labeled diagonally whereas this image has them labeled adjacent. Frustrated, I visited what I believe is the most authoritative site: the PDB (Protein Data Bank) which catalogs the x-ray crystal or NMR structures determined by research groups and found that the correct labeling is diagonal (as in the top diagram of this article). Thought you might like to know this. Thanks. 126lys ( talk) 19:09, 4 January 2011 (UTC)
The section about the oxidation state of iron in oxyhaemoglobin is wrong. It is now known that it is low-spin Fe(II). See Greenwood and Earshaw, Chemistry of the Elements 2nd edition, pp 1099-1100. The key point is that in deoxy-Hb the high-spin Fe(II) is too large to enter the plane of the porphirin ring (Figure 25.7) but when oxygen binds the low-spin Fe(II) enters the plane as it is small enough. The paramagnetism of O2 is destroyed because the Fe-O2 angle is 120o, so the pi-star orbitals are no longer doubly degenerate.
I'm not a biochemist, so I hesitate to edit the article myself. Petergans 09:56, 11 May 2007 (UTC)
-SBHarris, do you have reference for that? —Preceding
unsigned comment added by
216.80.44.45 (
talk)
02:06, 24 October 2008 (UTC)
Can we get a primary reference for the claim that IR frequencies change with the state of O2? For example is this Raman data or IR data? IR is usually not ideal for measuring absorption of diatomic molecules (though this may not be a problem for O2 coordinated with the hemoglobin). Jesse Greener ( talk) 19:40, 2 April 2010 (UTC)
Is it called hemoglobin or haemoglobin. The title says hemoglobin but in the opening line of the article it says haemoglobin. Which one should be changed? Ziphon 02:47, 29 May 2007 (UTC)
The original article was written in British English, and according to wikipedia rules, any form of english that is widely accepted is acceptable, so long that this was the original form the article took. Applying this, given the original article (tracking history back as far as i can) has the spelling 'haemoglobin', I move for this to be reinstated. 86.7.204.43 ( talk) 21:30, 30 August 2008 (UTC)
I come from more of a genetics background and knew hemoglobin in the context of the alpha globin locus, the beta globin locus and locus control region, the genes, etc. It took me forever to get my bearings here because "variants" refer to different combinations of protein subunits, not different protein subunits themselves. I now realize that α,β,etc. are the protein subunits, but I don't think this was explained very well and the protein subunits themselves definitely aren't talked about much. For now I'll just add links under "See also" to the genes, since I'm not sure on a good consistent nomenclature for the article. Forluvoft 06:52, 3 November 2007 (UTC)
The genetics of haemoglobin is quite complex and changes with the age of the embryo and child. None of the complexity is shown here. Please see the article on Fetal haemoglobin; http://en.wikipedia.org/wiki/Fetal_hemoglobin for a start. The genetics are also very interesting as the gene is really more of a region than a locus. Most of the sequence is coded forward but some is coded in reverse direction. Sequences are moved around as transcribed into mRNA and then other sequences are moved and deleted in the protein assembly. This synthesis is missing. 198.103.184.76 ( talk) —Preceding undated comment added 15:39, 11 March 2013 (UTC)
The "role in disease" section lists several diseases of "too little" or "broken" hemoglobin. What is it when you have too much hemoglobin? Polycythemia? Something else? WhatamIdoing ( talk) 03:55, 22 August 2008 (UTC)
I do not know much about the chemistry of hemoglobin and the like, but a section detailing how and why hemoglobin levels are measured in humans. A table or something illustrating the distribution and ideal hemoglobin level would also be great. My doctor just called me and all he said was 7 and I have absolutly no clue what that means. Google will answer me in minutes, but still, I was hoping Wikipedia would have it. --Crucible Guardian 6 July 2005 01:29 (UTC) —Preceding unsigned comment added by Ohiohealthquiz ( talk • contribs)
I don't know about this edit. If we've got a source that says 1851, then why are we replacing it with one that asserts a 1940 discovery? WhatamIdoing ( talk) 20:11, 8 January 2009 (UTC)
From the paragraph headed Research History:
Not a claim of discovery, but a fairly strong implication that someone else had already discovered hæmoglobin; granted, Engelhard did not use that term but instead called it vera materia sanguini purpureum colorem.
I found this on an American Chemical Society webpage ( https://www.acs.org/content/acs/en/molecule-of-the-week/archive/h/hemoglobin.html):
Here are some significant events in the history of hemoglobin discovery:
- 1825: J. F. Engelhard shows that the Fe/protein ratio is the same in several species’ hemoglobin.
- 1840: F. L. Hünefeld discovers that hemoglobin transports oxygen.
I think that makes "protein" a likely typo for "property of" in the bit about Hünefeld, but I do not have access to the primary sources. Regardless, for Engelhard to have come up with such a close (and, at the time, astonishing) estimate for the molecular mass of hæmoglobin deserves a much wider currency.
I'm going to make the edit and see what turns up. Moletrouser ( talk) 10:21, 23 September 2018 (UTC)
This is a very interesting article, with great information and graphics. However, I must comment that this page seems to require too much prior knowledge of biochemistry or medicine from the general reader, the presumed audience/user. For instance, why the presumption that the reader knows what an "erythrocyte" is? It would be arrogant to say, "Well, they can just look it up." That is poor editing if the intended audience is not limited to those with a chemical or biological major in college or medical school training. Why not at least define as "red blood cells"? Also, the inconsistent spelling of hemoglobin in the very heavy section "Presence in nonerythroid cells" is distracting and possibly confusing, if one didn`t know that that was all it was. Again, this article is impressive, esp. as it is "Scot-free"! (non-PC comment, LOL) Jack B108 ( talk) 02:03, 15 January 2010 (UTC)
If you find places where you find the techical level unevenness unusually bad, I suggest you fix it by adding introductory explanatory material to get from the level you feel comfortable at, to that of the present text. If doing so increases the length of this article so much that further spin-offs become necessary, that's fine! It will then trigger the WP:SS mechanism. So this is a natural mechanism of growth, and a self-regulating one when it comes to technical level. It's just that this sort of evolution occurs with less gradualism and uniformity than many people who are used to "non-grown" encyclopedias are comfortable with. S B H arris 02:57, 15 January 2010 (UTC)
This section gives a good account of the historical facts, but the conclusion is now known to be wrong - see Greenwood, Norman N.; Earnshaw, Alan (1997). Chemistry of the Elements (2nd ed.). Butterworth-Heinemann. ISBN 978-0-08-037941-8. p. 1099. Hb-O2 is a complex of low-spin iron(II) with the oxygen molecule. The angle Fe-O-O is not 180°. The non-linearity destroys the degeneracy of the π* orbitals and so the electrons which have paralell spins in the oxygen molecule can pair up in the complex at a lower energy cost than is required to form the singlet state in the isolated oxygen molecule. This section therefore need more attention than I feel qualified to give, as I'm not expert in biochemistry. Petergans ( talk) 14:12, 17 March 2010 (UTC)
Conversion between g/dl is given differently in different sections (quotes A and B below).
A) Each subunit has a molecular weight of about 17,000 daltons, for a total molecular weight of the tetramer of about 68,000 daltons (64,458 g/mol)[24]. Thus, 1 g/dL = 0.1551 mmol/L.
B) Hemoglobin concentration measurement is among the most commonly performed blood tests, usually as part of a complete blood count. For example it is typically tested before or after blood donation. Results are reported in g/L, g/dL or mol/L. 1 g/dL equals about 0.6206 mmol/L
The former is intuitively right as it uses to the full weight of tetrameric haemoglobin, but it is the latter (that gives the concentration of heme-groups, 1 per subunit of approximately 16000) that is consictent with my ADVIA outputs. Can anyone give me a reason for this discrepancy?
The article talks about the fact that glucose can bond to haemoglobin, and the diagnostic use of this, but doesn't mention a physiological role. Is there one? Why is haemoglobin able to combine with glucose? It would certainly help the article to either explain one, or to say that none is known, as most readers are bound to wonder about this. 144.32.126.16 ( talk) 10:03, 24 September 2010 (UTC)
It is not clear whether it is easier or more difficult for the fourth oxygen molecule to bind (as far as I know, it is more difficult) and the paragraph implies otherwise.
59.182.159.57 ( talk) 03:43, 25 October 2010 (UTC)
Based on a quick check of an online dictionary, the word "heme" was first used in 1925, well after the use of "hemoglobin". I would "guess" that the word is based on "hemo-" (blood) and "globin" (roundish protein) and was called that before heme was discovered, but I don't have a reference source to verify this. Anyone else have a specific reference for this? -- Kris ( talk) 17:18, 30 December 2011 (UTC)
Section: Oxygen saturation Narrative: "In general, hemoglobin can be saturated with oxygen molecules (oxyhemoglobin), or desaturated with oxygen molecules (deoxyhemoglobin)"
The phrase "desaturated with oxygen molecules" is difficult to parse. Does this simply mean "lacking in oxygen molecules", or does it mean "can be desaturated, by using oxygen molecules"? Pretty sure the former, but this is a very strange way to say so.
Also, is there no intermediate state of partially filled with oxygen molecules? — Preceding unsigned comment added by Gwideman ( talk • contribs) 18:35, 1 April 2013 (UTC)
The picture of heme shows the binding of CO2, but in many works is shown, that it is more probable of binding it to the amino ends of each four chains. Also the name carbamino is telling about the reaction CO2(carb) + -NH2(amino) = -NHCOOH more than Fe + CO2 = FeCO2+ or what it is? — Preceding unsigned comment added by MarekMatejak ( talk • contribs) 23:19, 26 June 2013 (UTC)
The comment(s) below were originally left at Talk:Hemoglobin/Comments, and are posted here for posterity. Following several discussions in past years, these subpages are now deprecated. The comments may be irrelevant or outdated; if so, please feel free to remove this section.
Very nicely done article: should need relatively little work to advance it to FA status. – Clockwork Soul |
Last edited at 21:06, 23 October 2006 (UTC). Substituted at 17:37, 29 April 2016 (UTC)
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The result of the move request was: no consensus to move the page to the proposed title at this time, per the discussion below. Dekimasu よ! 06:19, 5 August 2018 (UTC)
Hemoglobin → Haemoglobin – The preferred title has been discussed informally before, but it seems like it is time for a formal move discussion after a recent cut'n'paste move attempt. Haemoglobin is the traditional spelling, but hemoglobin is arguably now more common. See discussion above. Lithopsian ( talk) 11:30, 29 July 2018 (UTC)
Would anyone be opposed to me cleaning up and shortening the section on the oxidation state? It's all good information, but it's something of a rabbit hole that is probably not of interest (or accessible) to a general audience. I think it could all be summarized in a paragraph, pointing out the conflicting models and stating that there is disagreement about the matter. If there is general consensus to keep it the way it is, I'll shut up. WeirdNAnnoyed ( talk) 03:04, 18 April 2023 (UTC)
From this article:
From the article blood:
1060 kg/m3 = 106g per 100 mL
35% of 106g = 37g, well outside stated the range 12 to 20 grams
Sorry, I overlooked that 35% is for a blood cell, not blood as a whole.
Another thing, isn't it weird to give the density of blood in kg/m3? Wouldn't g/cm3 be more normal? 2A00:23C8:7B09:FA01:2165:E410:E554:7951 ( talk) 18:09, 25 February 2024 (UTC)