منابع مشابه
Action of plant proteinase inhibitors on enzymes of physiopathological importance.
Obtained from leguminous seeds, various plant proteins inhibit animal proteinases, including human, and can be considered for the development of compounds with biological activity. Inhibitors from the Bowman-Birk and plant Kunitz-type family have been characterized by proteinase specificity, primary structure and reactive site. Our group mostly studies the genus Bauhinia, mainly the species bau...
متن کاملDigestibility and Proteinase Inhibitory Action of a Kidney Bean Globulin
A globulin fraction, isolated from black beans (Phaseolus vulgaris), was resistant to hydrolysis by pepsin, trypsin, chymotrypsin, papain, ficin, hurain, and subtilisin. After denaturation of the globulin by heat or urea, only slight hydrolysis by enzymes could be detected. The activity of all seven proteinases on their respective substrates was inhibited by the bean globulin. Preincubation of ...
متن کاملModelling the action of proteinase and inhibitor in tissue invasion.
Tissue invasion processes have been receiving considerable attention in recent years. The successful invasion and subsequent implantation of a mammalian trophoblast into maternal uterine tissue is under the control of a self-regulating mechanism, as yet not fully determined, which if operating incorrectly can lead to the excessive placental invasion associated with choriocarcinoma or insufficie...
متن کاملThe proteinase: mucus proteinase inhibitor binding stoichiometry.
In the nanomolar enzyme and inhibitor concentration range, 1 mol of mucus proteinase inhibitor (MPI) inhibits 1 mol of neutrophil elastase, cathepsin G, trypsin, and chymotrypsin. In the micromolar concentration range, the enzyme:inhibitor binding stoichiometry is still 1:1 for elastase but shifts to 2:1 for the three other proteinases. These data could be confirmed by three nonenzymatic method...
متن کاملPotyviral NIa proteinase, a proteinase with novel deoxyribonuclease activity.
The NIa proteinase from pepper vein banding virus (PVBV) is a sequence-specific proteinase required for processing of viral polyprotein in the cytoplasm. It accumulates in the nucleus of the infected plant cell and forms inclusion bodies. The function of this protein in the nucleus is not clear. The purified recombinant NIa proteinase was active, and the mutation of the catalytic residues His-4...
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ژورنال
عنوان ژورنال: Nature
سال: 1971
ISSN: 0028-0836,1476-4687
DOI: 10.1038/234112b0