Activation of Intracellular Proteinases of Yeast
نویسندگان
چکیده
منابع مشابه
A study of two yeast proteinases.
Autolysis is a procedure frequently employed in the isolation of materials from yeast. Although the intracellular yeast proteinases play an important r81e in autolysis, these enzymes have not been characterized by using up to date methods of analysis, and the existing literature concerning yeast proteinases presents conflicting results. In 1917, Dernby (1) reported that yeast contains two prote...
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A mutation of yeast pai1 has been isolated which leads to altered regulation of proteinase A inhibitor activity. Under conditions of derepression, this mutant as compared with wild type has a 70% reduction in proteinase A inhibitor activity, but no change in the activities of proteinase A or B. The growth of strains carrying the pai1 mutation is sensitive to temperature and pH. The altered phys...
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Prochymosin can be converted into chymosin by an action of external proteinases. Thus, thermolysin at pH 5.05 converts calf prochymosin into active Phe-chymosin, which is one amino acid longer than chymosin from the N-terminus with a yield of 73%. Even better results were achieved with prochymosin activation by Legionella pneumophila metalloproteinase. Apparently the stretch of prochymosin poly...
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Matrix metalloproteinases (MMPs) are zinc-containing proteinases that participate in tissue remodeling under physiological and pathological conditions. To test the involvement of bacterial proteinases in tissue injury during bacterial infections, we investigated the activation potential of various bacterial proteinases against precursors of MMPs (proMMPs) purified from human neutrophils (proMMP...
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LPS induces an up-regulation of promatrix metalloproteinase-9 (proMMP9) gene expression in cells of the monocyte/macrophage lineage. We demonstrate here that LPS preparations are also able to activate proMMP9 made by human macrophages or THP-1 cells via LPS-associated proteinases, which cleave the N-terminal propeptide at a site or sites close to the one cleaved upon activation with organomercu...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1968
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.32.359