Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes
نویسندگان
چکیده
منابع مشابه
comparison of catalytic activity of heteropoly compounds in the synthesis of bis(indolyl)alkanes.
heteropoly acids (hpa) and their salts have advantages as catalysts which make them both economically and environmentally attractive, strong br?nsted acidity, exhibiting fast reversible multi-electron redox transformations under rather mild conditions, very high solubility in polar solvents, fairly high thermal stability in the solid states, and efficient oxidizing ability, so that they are imp...
15 صفحه اولA fluorometric determination of trypsin-like amidase activity and activity of trypsin inhibitors in serum.
The activity of crystalline trypsin and the trypsin-like amidase activity and the activity of trypsin inhibitors in serum were measured fluorometically, with a-benzoyl--L-arginine--na phthylamide (BANA) as substrate. The method is simpler and more sensitive than the colorimetric method based on the Bratton-Marshall reaction. Serum of pancreatectomized dogs hydrolyzed BANA at a significant rate,...
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cement is an essential ingredient in the concrete buildings. for production of cement considerable amount of fossil fuel and electrical energy is consumed. on the other hand for generating one tone of portland cement, nearly one ton of carbon dioxide is released. it shows that 7 percent of the total released carbon dioxide in the world relates to the cement industry. considering ecological issu...
The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites.
Proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites. Previous studies suggest a complex network of allosteric interactions between these catalytic and multiple regulatory sites. We used positional scanning combinatorial substrate libraries to determine the ...
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ژورنال
عنوان ژورنال: Chemistry & Biology
سال: 1999
ISSN: 1074-5521
DOI: 10.1016/s1074-5521(99)80036-2