Renal tissue
kallikrein is formed from
kidney tissue
prokallikrein by activation with the enzyme
trypsin. It
catalyses the
chemical reaction causing preferential cleavage of Arg- bonds in small molecule substrates, acting to highly selectively release
kallidin (lysyl-bradykinin, a bioactive
kinin) from
kininogen (a kinin protein precursor).
^Pesquero JL, Boschcov P, Oliveira MC, Paiva AC (October 1982). "Effect of substrate size on tonin activity". Biochemical and Biophysical Research Communications. 108 (4): 1441–6.
doi:
10.1016/s0006-291x(82)80068-5.
PMID6295383.
^Gutkowska J, Corvol P, Figueiredo AF, Inagami T, Bouhnik J, Genest J (1984). "Kinetic studies of rat renin and tonin on purified rat angiotensinogen". Canadian Journal of Biochemistry and Cell Biology. 62 (2–3): 137–42.
doi:
10.1139/o84-020.
PMID6097352.
^Kato H, Enjyoji K, Miyata T, Hayashi I, Oh-ishi S, Iwanaga S (February 1985). "Demonstration of arginyl-bradykinin moiety in rat HMW kininogen: direct evidence for liberation of bradykinin by rat glandular kallikreins". Biochemical and Biophysical Research Communications. 127 (1): 289–95.
doi:
10.1016/s0006-291x(85)80157-1.
PMID3844939.
^Fujinaga M, James MN (May 1987). "Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution". Journal of Molecular Biology. 195 (2): 373–96.
doi:
10.1016/0022-2836(87)90658-9.
PMID2821276.
^Kato H, Nakanishi E, Enjyoji K, Hayashi I, Oh-ishi S, Iwanaga S (December 1987). "Characterization of serine proteinases isolated from rat submaxillary gland: with special reference to the degradation of rat kininogens by these enzymes". Journal of Biochemistry. 102 (6): 1389–404.
doi:
10.1093/oxfordjournals.jbchem.a122185.
PMID3482210.
Renal tissue
kallikrein is formed from
kidney tissue
prokallikrein by activation with the enzyme
trypsin. It
catalyses the
chemical reaction causing preferential cleavage of Arg- bonds in small molecule substrates, acting to highly selectively release
kallidin (lysyl-bradykinin, a bioactive
kinin) from
kininogen (a kinin protein precursor).
^Pesquero JL, Boschcov P, Oliveira MC, Paiva AC (October 1982). "Effect of substrate size on tonin activity". Biochemical and Biophysical Research Communications. 108 (4): 1441–6.
doi:
10.1016/s0006-291x(82)80068-5.
PMID6295383.
^Gutkowska J, Corvol P, Figueiredo AF, Inagami T, Bouhnik J, Genest J (1984). "Kinetic studies of rat renin and tonin on purified rat angiotensinogen". Canadian Journal of Biochemistry and Cell Biology. 62 (2–3): 137–42.
doi:
10.1139/o84-020.
PMID6097352.
^Kato H, Enjyoji K, Miyata T, Hayashi I, Oh-ishi S, Iwanaga S (February 1985). "Demonstration of arginyl-bradykinin moiety in rat HMW kininogen: direct evidence for liberation of bradykinin by rat glandular kallikreins". Biochemical and Biophysical Research Communications. 127 (1): 289–95.
doi:
10.1016/s0006-291x(85)80157-1.
PMID3844939.
^Fujinaga M, James MN (May 1987). "Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution". Journal of Molecular Biology. 195 (2): 373–96.
doi:
10.1016/0022-2836(87)90658-9.
PMID2821276.
^Kato H, Nakanishi E, Enjyoji K, Hayashi I, Oh-ishi S, Iwanaga S (December 1987). "Characterization of serine proteinases isolated from rat submaxillary gland: with special reference to the degradation of rat kininogens by these enzymes". Journal of Biochemistry. 102 (6): 1389–404.
doi:
10.1093/oxfordjournals.jbchem.a122185.
PMID3482210.