Results 21 to 30 of about 341,861 (262)

Measurement of the Proteinase Inhibitors of the Bovine Pancreas by Radioimmunoassay [PDF]

open access: yes, 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
core   +1 more source

Pancreatic secretory trypsin inhibitor: More than a trypsin inhibitor

open access: yesWorld 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
openaire   +3 more sources

ISOLATION FROM BEEF PANCREAS OF CRYSTALLINE TRYPSINOGEN, TRYPSIN, A TRYPSIN INHIBITOR, AND AN INHIBITOR-TRYPSIN COMPOUND [PDF]

open access: yesJournal 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
openaire   +3 more sources

Differential in vitro and in vivo effect of barley cysteine and serine protease inhibitors on phytopathogenic microorganisms [PDF]

open access: yes, 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
core   +2 more sources

Characterization and pharmacological properties of a novel multifunctional Kunitz inhibitor from Erythrina velutina seeds. [PDF]

open access: yesPLoS ONE, 2013
Inhibitors of peptidases isolated from leguminous seeds have been studied for their pharmacological properties. The present study focused on purification, biochemical characterization and anti-inflammatory and anticoagulant evaluation of a novel Kunitz ...
Richele J A Machado   +11 more
doaj   +1 more source

The impact of physiological stress conditions on protein structure and trypsin inhibition of serine protease inhibitor Kazal type 1 (SPINK1) and its N34S variant [PDF]

open access: yes, 2020
One of the most common mutations in the serine protease inhibitor Kazal type 1 (SPINK1) gene is the N34S variant which is strongly associated with chronic pancreatitis. Although it is assumed that N34S mutation constitutes a high-risk factor, the underlying pathologic mechanism is still unknown.
arxiv   +1 more source

Multisecond ligand dissociation dynamics from atomistic simulations [PDF]

open access: yesNat. Commun. 11, 2918 (2020), 2020
Coarse-graining of fully atomistic molecular dynamics simulations is a long-standing goal in order to allow the description of processes occurring on biologically relevant timescales. For example, the prediction of pathways, rates and rate-limiting steps in protein-ligand unbinding is crucial for modern drug discovery. To achieve the enhanced sampling,
arxiv   +1 more source

Calorimetry of Some Trypsin-Trypsin Inhibitor Reactions

open access: yesJournal of Biological Chemistry, 1972
The heats of reaction of trypsin with soybean (Kunitz), ovomucoid, and lima bean inhibitors have been measured at pH 5.0 and 10° and 25°. All the reactions were endothermic, with ΔH ranging from 8.6 Cal per mole for the lima bean inhibitor to 15.3 Cal per mole for the soybean inhibitor. Equilibrium constants for the association were calculated from the
Robert J. Baugh, C.G. Trowbridge
openaire   +3 more sources

Trypsin Inhibitor in Wholewheat Flour [PDF]

open access: yesNature, 1961
PRELIMINARY work on a trypsin inhibitor in wholewheat flour was reported by Shyamala1. A crude concentrate containing the trypsin inhibitor was prepared by the ‘ammonium sulphate’ method of Borchers et al.2 modified by Lyman3 as follows:
R. L. Lyman   +2 more
openaire   +3 more sources

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