Results 11 to 20 of about 261,497 (358)
Developments in plant breeding for improved nutritional quality of soya beans II. Anti-nutritional factors [PDF]
, 2000 Nutritional value of most plant materials is limited by the presence of numerous naturally occurring compounds which interfere with nutrient digestion and absorption.
Clarke, E, Wiseman, J
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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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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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Trypsin inhibition by macrocyclic and open-chain variants of the squash inhibitor MCoTI-II [PDF]
, 2005 MCoTl-I and MCoTl-II from the seeds of Momordica cochinchinensis are inhibitors of trypsin-like proteases and the only known members of the large family of squash inhibitors that are cyclic and contain an additional loop connecting the amino- and the ...
Avrutina, Olga +6 more
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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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Trypsin inhibitors in turnip (Brassica rapa L.) seeds
Acta Societatis Botanicorum Poloniae, 2014 A method of trypsin inhibitors isolation from turnip seeds is described. Inhibitors were extracted with 0.01 N HCI, concentrated by salting out with ammonium sulfate, and purified using ion-exchange chromatography on Sp-Sephadex C-25, QAE-Sephadex A-25 ...
Anna Wilimowska-Pelc
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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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Influence of Different Genotypes on Trypsin Inhibitor Levels and Activity in Soybeans
Sensors, 2007 This study describes the relationship between the two major trypsin inhibitors (TI) in soybean, i.e., the Kunitz (KTI) and Bowman-Birk (BBI) trypsin inhibitors, as well as between them and the corresponding trypsin inhibitor activity (TIA).
Viktor A. Nedovic +4 more
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Calorimetry of Some Trypsin-Trypsin Inhibitor Reactions
Journal 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
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