Napin is one of the two most abundant seed storage proteins in the seeds of dicot crop mustard and rapeseed ( Brassica napus L., B. juncea L. Czern., B. nigra L. W.D.J.Koch, B. rapa L. and Sinapis alba L.). [1] [2] They are water soluble low-molecular weight basic proteins classified as 2S or 1.7S proteins, representing 20–40% of total seed protein, and having a molecular weight in the range of 12–17 kDa. [3] [4] Their isoelectric point varies based on the method of extraction and the specific characteristics of the isoforms that exist. They are composed of two polypeptide chains, a 4.5 kDa small subunit and a large 10 kDa subunit, stabilized primarily by disulphide bonds. Their secondary structure shows a high α-helical content. [5]
Arginine, lysine, and cysteine make napines excellent antibacterials, and since it's a basic protein, it can change its acidity to make it more effective. [6] Some in silico and in vitro antimicrobial activity screening reported napins as antimicrobial [5] [7] [2] and antifungal peptides. [8] [9]
As a basic protein, napin can be used to bind together and determine the shape, properties, and be able to synthesize when seeds develop. [10]
In terms of molecular weights, napin polypeptide chains are made up of 9,900 and 4,000 amino acids held together by disulfide bonds .The amino acid sequence of napin cDNA clones and napin peptide fragments indicate napin starts as a 178-residue precursor. [10]
Napin is water soluble and soluble in a wide pH range. [11]
- ^ Rahman, M. (2018). "Brassicaceae mustards: Traditional and agronomic uses in Australia and New Zealand". Molecules. 23 (1): 231. doi: 10.3390/molecules23010231. PMC 6017612. PMID 29361740.
- ^ a b Rahman, M. (2020). Identification, Molecular and Proteomic Characterisation of Brassica rapa Seed Storage Proteins with Allergenic and Antimicrobial Potential (Thesis). Southern Cross University, Australia.
-
^ Rahman, M. (2000).
"In Silico, Molecular Docking and In Vitro Antimicrobial Activity of the Major Rapeseed Seed Storage Proteins". Frontiers in Pharmacology. 11: 1340.
doi:
10.3389/fphar.2020.01340.
PMC
7508056.
PMID
33013372.
This article incorporates text available under the
CC BY 4.0 license.
- ^ Rahman, M. (2000). "Identification, characterization and epitope mapping of proteins encoded by putative allergenic napin genes from Brassica rapa". Clinical and Experimental Allergy. 50 (7): 848–868. doi: 10.1111/cea.13612. PMID 32306538. S2CID 216029445.
- ^ a b Rahman, M. (2000). "In Silico, Molecular Docking and In Vitro Antimicrobial Activity of the Major Rapeseed Seed Storage Proteins". Frontiers in Pharmacology. 11: 1340. doi: 10.3389/fphar.2020.01340. PMC 7508056. PMID 33013372.
- ^ Cheung, LamLam (December 2013). The Emulsifying Properties of Cruciferin Rich and Napin Rich Protein Isolates From Brassica Napus L (Master of Science thesis). University of Saskatchewan. CiteSeerx: 10.1.1.848.5181.
-
^ Munir, A. (2000).
"In silico studies and functional characterization of a napin protein from seeds of Brassica juncea" (PDF). International Journal of Agriculture and Biology. 19–1092.
doi:
10.17957/IJAB/15.1247 (inactive 31 January 2024).
{{ cite journal}}: CS1 maint: DOI inactive as of January 2024 ( link) - ^ Mignone, G. (2022). "Isolation of the mustard Napin protein Allergen Sin a 1 and characterisation of its antifungal activity". Biochemistry and Biophysics Reports. 29 (101208): 101208. doi: 10.1016/j.bbrep.2022.101208. PMC 8777239. PMID 35079640.
- ^ Jyothi, T. C. (2007). "Napin from Brassica juncea: Thermodynamic and structural analysis of stability". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1774 (7): 907–919. doi: 10.1016/j.bbapap.2007.04.008. PMID 17544981.
- ^ a b Ericson, M. L.; Rödin, J.; Lenman, M.; Glimelius, K.; Josefsson, L. G.; Rask, L. (1986-11-05). "Structure of the rapeseed 1.7 S storage protein, napin, and its precursor". The Journal of Biological Chemistry. 261 (31): 14576–14581. doi: 10.1016/S0021-9258(18)66909-1. ISSN 0021-9258. PMID 3771543.
- ^ Perera, Suneru P.; McIntosh, Tara C.; Wanasundara, Janitha P. D. (2016-09-07). "Structural Properties of Cruciferin and Napin of Brassica napus (Canola) Show Distinct Responses to Changes in pH and Temperature". Plants. 5 (3): E36. doi: 10.3390/plants5030036. ISSN 2223-7747. PMC 5039744. PMID 27618118.
 | This protein-related article is a stub. You can help Wikipedia by expanding it. |
Napin is one of the two most abundant seed storage proteins in the seeds of dicot crop mustard and rapeseed ( Brassica napus L., B. juncea L. Czern., B. nigra L. W.D.J.Koch, B. rapa L. and Sinapis alba L.). [1] [2] They are water soluble low-molecular weight basic proteins classified as 2S or 1.7S proteins, representing 20–40% of total seed protein, and having a molecular weight in the range of 12–17 kDa. [3] [4] Their isoelectric point varies based on the method of extraction and the specific characteristics of the isoforms that exist. They are composed of two polypeptide chains, a 4.5 kDa small subunit and a large 10 kDa subunit, stabilized primarily by disulphide bonds. Their secondary structure shows a high α-helical content. [5]
Arginine, lysine, and cysteine make napines excellent antibacterials, and since it's a basic protein, it can change its acidity to make it more effective. [6] Some in silico and in vitro antimicrobial activity screening reported napins as antimicrobial [5] [7] [2] and antifungal peptides. [8] [9]
As a basic protein, napin can be used to bind together and determine the shape, properties, and be able to synthesize when seeds develop. [10]
In terms of molecular weights, napin polypeptide chains are made up of 9,900 and 4,000 amino acids held together by disulfide bonds .The amino acid sequence of napin cDNA clones and napin peptide fragments indicate napin starts as a 178-residue precursor. [10]
Napin is water soluble and soluble in a wide pH range. [11]
- ^ Rahman, M. (2018). "Brassicaceae mustards: Traditional and agronomic uses in Australia and New Zealand". Molecules. 23 (1): 231. doi: 10.3390/molecules23010231. PMC 6017612. PMID 29361740.
- ^ a b Rahman, M. (2020). Identification, Molecular and Proteomic Characterisation of Brassica rapa Seed Storage Proteins with Allergenic and Antimicrobial Potential (Thesis). Southern Cross University, Australia.
-
^ Rahman, M. (2000).
"In Silico, Molecular Docking and In Vitro Antimicrobial Activity of the Major Rapeseed Seed Storage Proteins". Frontiers in Pharmacology. 11: 1340.
doi:
10.3389/fphar.2020.01340.
PMC
7508056.
PMID
33013372.
This article incorporates text available under the
CC BY 4.0 license.
- ^ Rahman, M. (2000). "Identification, characterization and epitope mapping of proteins encoded by putative allergenic napin genes from Brassica rapa". Clinical and Experimental Allergy. 50 (7): 848–868. doi: 10.1111/cea.13612. PMID 32306538. S2CID 216029445.
- ^ a b Rahman, M. (2000). "In Silico, Molecular Docking and In Vitro Antimicrobial Activity of the Major Rapeseed Seed Storage Proteins". Frontiers in Pharmacology. 11: 1340. doi: 10.3389/fphar.2020.01340. PMC 7508056. PMID 33013372.
- ^ Cheung, LamLam (December 2013). The Emulsifying Properties of Cruciferin Rich and Napin Rich Protein Isolates From Brassica Napus L (Master of Science thesis). University of Saskatchewan. CiteSeerx: 10.1.1.848.5181.
-
^ Munir, A. (2000).
"In silico studies and functional characterization of a napin protein from seeds of Brassica juncea" (PDF). International Journal of Agriculture and Biology. 19–1092.
doi:
10.17957/IJAB/15.1247 (inactive 31 January 2024).
{{ cite journal}}: CS1 maint: DOI inactive as of January 2024 ( link) - ^ Mignone, G. (2022). "Isolation of the mustard Napin protein Allergen Sin a 1 and characterisation of its antifungal activity". Biochemistry and Biophysics Reports. 29 (101208): 101208. doi: 10.1016/j.bbrep.2022.101208. PMC 8777239. PMID 35079640.
- ^ Jyothi, T. C. (2007). "Napin from Brassica juncea: Thermodynamic and structural analysis of stability". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1774 (7): 907–919. doi: 10.1016/j.bbapap.2007.04.008. PMID 17544981.
- ^ a b Ericson, M. L.; Rödin, J.; Lenman, M.; Glimelius, K.; Josefsson, L. G.; Rask, L. (1986-11-05). "Structure of the rapeseed 1.7 S storage protein, napin, and its precursor". The Journal of Biological Chemistry. 261 (31): 14576–14581. doi: 10.1016/S0021-9258(18)66909-1. ISSN 0021-9258. PMID 3771543.
- ^ Perera, Suneru P.; McIntosh, Tara C.; Wanasundara, Janitha P. D. (2016-09-07). "Structural Properties of Cruciferin and Napin of Brassica napus (Canola) Show Distinct Responses to Changes in pH and Temperature". Plants. 5 (3): E36. doi: 10.3390/plants5030036. ISSN 2223-7747. PMC 5039744. PMID 27618118.
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