Natural occurrence and chemical modification of proteinase B inhibitors from yeast.
نویسندگان
چکیده
منابع مشابه
Isolation and properties of two inhibitors of proteinase B from yeast.
In continuation of our studies on the inactivation of tryptophan synthase from Saccharomyces cerevisiae by proteinases from the same organism, two protein inhibitors of the tryptophan synthase inactivating yeast proteinase B were purified from boiled bakers’ yeast extract. The molecular weight of both inhibitors is 10,000 and both inhibit specifically proteinase B, but not proteinases A and C. ...
متن کاملextraction and acetylation of purified trypsin from bovin pancreas and study of some its physico-chemical properties
آنزیم تریپسین در شرایط قلیایی ناپایدار می باشد .و فعالیت پروتئولیتیکی تریپسین منجربه خود هضمی آن در جایگاههای خاصی می گردد. بنابر این آنزیمی با ناپایداری بالا محسوب میگردد. در سالهای اخیر موفق شدند که با ایجاد تغیرات شیمیایی با اضافه کردن فلزات خاص ، کلسیم و یا عمل استیلاسیون منجر به افزایش پایداری آنزیم تریپسین گردند. مطالعات در حال حاضر نشان می دهد که تریپسین استیله شده فعالیت آنزیمی خود را ...
15 صفحه اولPurification and properties of proteinase B from yeast.
Proteinase B (EC 3.4.22.9) was purified from commercial baker's yeast and from wild type strains of Saccharomyces cerevisiae and Saccharomyces carlsbergensis. For large scale purification a procedure was developed involving hydrophobic chromatography on octyl-Sepharose 4B and gel filtration on Sephadex G-100. A rapid purification of small amounts of proteinase B was achieved by affinity chromat...
متن کاملPurification and molecular characterization of two inhibitors of yeast proteinase B.
A rapid purification procedure for large scale preparations of yeast proteinase B inhibitors 1 and 2 (IB1 and IB2) is described. By disc gel electrophoresis, amino acid analysis, and end-group determinations, each of the inhibitors is homogeneous. Both inhibitors are polypeptides with molecular weights of 8,500, containing 74 residues. No components other than amino acids could be detected. The...
متن کاملChemical modification of yeast 3-phosphoglycerate kinase.
Sulfhydryl reagents, as well as mild hydrogen peroxide oxidation, do not inhibit the activity of yeast phosphoglycerate kinase, indicating that the single thiol group and 3 methionine residues present in the enzyme are not essential for activity. Nitration of phosphoglycerate kinase by tetranitromethane inhibits the enzyme by reaction with a single tyrosine residue. Substrates provide partial p...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)63349-1