Results 11 to 20 of about 353,545 (343)
The occurrence of a trypsin inhibitor in brain [PDF]
Biochemical Journal, 1967 1. The tryptic hydrolysis of benzoyl-dl-argininyl-beta-naphthylamide is inhibited by homogenates of human and ox brain. 2. The inhibitor is associated primarily with the membranous portion of the particulate matter, and is not found in the 90000g supernatant fraction. 3. The reaction of the inhibitor with trypsin is rapid. 4.
A. S. Brecher, N. M. Quinn
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Pancreatic trypsin inhibitor. 2. Reaction with trypsin [PDF]
Biochemical Journal, 1953 N. M. Green, Elizabeth Work
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The Reactive Site of Trypsin Inhibitors
Journal of Biological Chemistry, 1966 Virgin soybean trypsin inhibitor has 1 NH2-terminal aspartic acid or asparagine residue and no COOH-terminal residues that can be released by carboxypeptidase B. Upon incubation with 1 mole % of trypsin for 24 hours at pH 3.75, virgin inhibitor is converted to a modified inhibitor which has 2 NH2 terminals aspartic acid or asparagine and isoleucine ...
Kyoichi Ozawa, M. Laskowski
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Engineering trypsin for inhibitor resistance [PDF]
Protein Science, 2015 AbstractThe development of effective protease therapeutics requires that the proteases be more resistant to naturally occurring inhibitors while maintaining catalytic activity. A key step in developing inhibitor resistance is the identification of key residues in protease‐inhibitor interaction. Given that majority of the protease therapeutics currently
Teaster Baird +4 more
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Kinetic and thermodynamic analysis of leech-derived tryptase inhibitor interaction with bovine tryptase and bovine trypsin [PDF]
, 2000 The interaction of leech-derived tryptase inhibitor (LDTI) with bovine liver capsule tryptase (BLCT) and bovine trypsin has been studied using both thermodynamic and kinetic approaches.
Auerswald E.A. +6 more
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Measurement of the Proteinase Inhibitors of the Bovine Pancreas by Radioimmunoassay [PDF]
, 1976 Bovine pancreas contains two polypeptide trypsin inhibitors that are not homologous and differ in their inhibitory activity towards chymotrypsin, kallikrein, elastase, and other serine proteinases. The Kunitz inhibitor and the Kazal inhibitor are present
Fink, Edwin +2 more
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ISOLATION FROM BEEF PANCREAS OF CRYSTALLINE TRYPSINOGEN, TRYPSIN, A TRYPSIN INHIBITOR, AND AN INHIBITOR-TRYPSIN COMPOUND [PDF]
Journal of General Physiology, 1936 Methods are described for the isolation and crystallization of trypsinogen, trypsin, a substance which inhibits trypsin, and an inhibitor-trypsin compound. Analyses and some of the properties of these compounds are given.
John H. Northrop, M. Kunitz
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HUMAN SEMINAL TRYPSIN INHIBITORS [PDF]
Reproduction, 1972 Summary. The presence of trypsin inhibitors in human seminal plasma was demonstrated, and their effect on the acrosomal trypsin-like enzyme (TLE), as well as on other proteolytic enzymes, was studied. Two inhibitor fractions with approximate molecular weights of 11,500 and 4000 were obtained by gel filtration.
J. J. O. Suomine, M. Niemi
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Pancreatic secretory trypsin inhibitor: More than a trypsin inhibitor
World Journal of Gastrointestinal Pathophysiology, 2010 Kazal-type serine protease inhibitor is one of the most important and widely distributed protease inhibitor families. Pancreatic secretory trypsin inhibitor (PSTI), also known as serine protease inhibitor Kazal type I(SPINK1), binds rapidly to trypsin, inhibits its activity and is likely to protect the pancreas from prematurely activated trypsinogen ...
Cun-Shuan Xu, Gai-Ping Wang
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Differential in vitro and in vivo effect of barley cysteine and serine protease inhibitors on phytopathogenic microorganisms [PDF]
, 2011 Protease inhibitors from plants have been involved in defence mechanisms against pests and pathogens. Phytocystatins and trypsin/α-amylase inhibitors are two of the best characterized protease inhibitor families in plants.
Cambra Marin, Ines +5 more
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