Results 11 to 20 of about 364,327 (313)
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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Agriculture, 2023 Trypsin inhibitors (TIs) in soybean seeds reduce the availability of processed soybean foods and animal feed. This study aimed to evaluate the trypsin inhibitor activity (TIA) in 999 Korean soybean accessions and conduct molecular characterization of ...
Aron Park +9 more
doaj +1 more source
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
core +1 more source
CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR [PDF]
Journal of General Physiology, 1946 A study has been made of the general properties of crystalline soybean trypsin inhibitor. The soy inhibitor is a stable protein of the globulin type of a molecular weight of about 24,000. Its isoelectric point is at pH 4.5. It inhibits the proteolytic action approximately of an equal weight of crystalline trypsin by combining with trypsin to form a ...
openaire +4 more sources
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
core +2 more sources
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 ...
Gai-Ping, Wang, Cun-Shuan, Xu
openaire +2 more sources
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
core +1 more source
Journal of Applied Sciences and Environmental Management, 2010 Legumes are an important source of protein in many developing countries. However this protein is not readily available because of antinutrients. Farmers are being encouraged to grow bambara groundnut to meet food sufficiency, hence information on the ...
O Tibe, JO Amarteifio
doaj +1 more source
The effects of nitrogen on protein, oil and trypsin inhibitor content of soybean [PDF]
, 2009 Nitrogen fertilization have influence on protein, oil and trypsin inhibitor content of different soybean genotypes. Seed protein content was increased over control by 60 kg ha-1 nitrogen while trypsin inhibitor was reduced by all treatmens (30, 60,90 N ...
Jankuloski Ljupcho +6 more
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Tyrosine sulfation of human trypsin steers S2' subsite selectivity towards basic amino acids. [PDF]
PLoS ONE, 2014 Human cationic and anionic trypsins are sulfated on Tyr154, a residue which helps to shape the prime side substrate-binding subsites. Here, we used phage display technology to assess the significance of tyrosine sulfation for the specificity of human ...
András Szabó +4 more
doaj +1 more source