Some properties of leucine aminopeptidase from Aspergillus japonica as a metalloenzyme.
نویسندگان
چکیده
منابع مشابه
extraction 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 ...
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Compounds consisting of the catechol group con nected to an amino acid or a small peptide only re cently have been the subject of few papers concern ing their structure-activity relationship. A number of 2,3-dihydroxybenzoic acid amides such as polyamine derivatives: parabactin [1 ], agrobactin [2], vibriobactin [3], or amino acid derivatives: glycine [4], lysine [5], serine [6 ], and threon...
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in this thesis, at first we investigate the bounded inverse theorem on fuzzy normed linear spaces and study the set of all compact operators on these spaces. then we introduce the notions of fuzzy boundedness and investigate a new norm operators and the relationship between continuity and boundedness. and, we show that the space of all fuzzy bounded operators is complete. finally, we define...
15 صفحه اولLeucine aminopeptidase fragments from an ascites tumor.
By 1946 (4) about 35 enzymes had been isolated and crystallized, and the controversy over their chemical nature was resolved with the conclusion that all enzymes contained a protein component essential for their activity. In 1951, however, Binkley (5-7) claimed to have purified highly active peptidases which analyzed as polynucleotides and were free from protein. His procedure was designed to e...
متن کاملLeucine Aminopeptidase (Bovine Lens)
The stability to pH and denaturing agents of crystalline leutine aminopeptidase (bovine lens) (EC 3.4.1.1) is reported. The native enzyme exhibited a molecular weight of 327,000. In 7 M urea below pH 3 and in 23.7 M guanidinium chloride below pH 8.5, both leucine aminopeptidase and its reduced and carboxamidomethylated derivative exhibited a molecular weight on equilibrium centrifugation of 54,...
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ژورنال
عنوان ژورنال: Chemical and Pharmaceutical Bulletin
سال: 1978
ISSN: 0009-2363,1347-5223
DOI: 10.1248/cpb.26.3101