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A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein

Lilja, H. LU orcid (1985) In Journal of Clinical Investigation 76(5). p.1899-1903
Abstract

A 33-kD glycoprotein, known as the 'prostate-specific antigen', was purified to homogeneity from human seminal plasma. The prostatic protein was identified as a serine protease, and its NH2-terminal sequence strongly suggests that it belongs to the family of glandular kallikreins. The structural protein of human seminal coagulum, the predominant protein in seminal vesicle secretion, was rapidly cleaved by the prostatic enzyme, which suggests that this seminal vesicle protein may serve as the physiological substrate for the protease. The prostatic enzyme hydrolyzed arginine- and lysine-containing substrates with a distinct preference for the former. All synthetic substrates tested were poor substrates for the enzyme. Synthetic... (More)

A 33-kD glycoprotein, known as the 'prostate-specific antigen', was purified to homogeneity from human seminal plasma. The prostatic protein was identified as a serine protease, and its NH2-terminal sequence strongly suggests that it belongs to the family of glandular kallikreins. The structural protein of human seminal coagulum, the predominant protein in seminal vesicle secretion, was rapidly cleaved by the prostatic enzyme, which suggests that this seminal vesicle protein may serve as the physiological substrate for the protease. The prostatic enzyme hydrolyzed arginine- and lysine-containing substrates with a distinct preference for the former. All synthetic substrates tested were poor substrates for the enzyme. Synthetic Factor XI(a) substrate (pyroglutamyl-prolyl-arginine-p-nitroanilide), and the synthetic kallikrein substrate (H-D-prolyl-phenylalanyl-arginine-p-nitroanilide) were hydrolyzed with maximum specific activities at 23°C of 79 and 34 nmol/min per mg and K(m) values of 1.0 and 0.45 mM, respectively. Synthetic substrates for plasmin, chymotrypsin, and elastase were either not hydrolyzed by the enzyme at all, or only hydrolyzed very slowly.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Clinical Investigation
volume
76
issue
5
pages
1899 - 1903
publisher
The American Society for Clinical Investigation
external identifiers
  • scopus:0022357088
  • pmid:3902893
ISSN
0021-9738
DOI
10.1172/JCI112185
language
English
LU publication?
yes
id
87ff7009-c17c-4cf3-8d79-b2656960b68a
date added to LUP
2022-12-06 16:52:04
date last changed
2024-04-04 12:15:25
@article{87ff7009-c17c-4cf3-8d79-b2656960b68a,
  abstract     = {{<p>A 33-kD glycoprotein, known as the 'prostate-specific antigen', was purified to homogeneity from human seminal plasma. The prostatic protein was identified as a serine protease, and its NH<sub>2</sub>-terminal sequence strongly suggests that it belongs to the family of glandular kallikreins. The structural protein of human seminal coagulum, the predominant protein in seminal vesicle secretion, was rapidly cleaved by the prostatic enzyme, which suggests that this seminal vesicle protein may serve as the physiological substrate for the protease. The prostatic enzyme hydrolyzed arginine- and lysine-containing substrates with a distinct preference for the former. All synthetic substrates tested were poor substrates for the enzyme. Synthetic Factor XI(a) substrate (pyroglutamyl-prolyl-arginine-p-nitroanilide), and the synthetic kallikrein substrate (H-D-prolyl-phenylalanyl-arginine-p-nitroanilide) were hydrolyzed with maximum specific activities at 23°C of 79 and 34 nmol/min per mg and K(m) values of 1.0 and 0.45 mM, respectively. Synthetic substrates for plasmin, chymotrypsin, and elastase were either not hydrolyzed by the enzyme at all, or only hydrolyzed very slowly.</p>}},
  author       = {{Lilja, H.}},
  issn         = {{0021-9738}},
  language     = {{eng}},
  number       = {{5}},
  pages        = {{1899--1903}},
  publisher    = {{The American Society for Clinical Investigation}},
  series       = {{Journal of Clinical Investigation}},
  title        = {{A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein}},
  url          = {{http://dx.doi.org/10.1172/JCI112185}},
  doi          = {{10.1172/JCI112185}},
  volume       = {{76}},
  year         = {{1985}},
}