Biochemical properties and primary structure of elastase inhibitor AFUEI from Aspergillus fumigatus
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چکیده
منابع مشابه
Biochemical properties and primary structure of elastase inhibitor AFUEI from Aspergillus fumigatus.
An elastase inhibitor from Aspergillus fumigatus (AFUEI) was isolated, and its biochemical properties and primary structure examined. The inhibitor was purified by column chromatography using DE52 cellulose and Sephadex G-75, and was found to be homogeneous as indicated by a single band following discontinuous PAGE and SDS-PAGE. A molecular mass of 7525.1 Da was observed by matrix-assisted deso...
متن کاملX-ray structure analysis and characterization of AFUEI, an elastase inhibitor from Aspergillus fumigatus.
Elastase from Aspergillus sp. is an important factor for aspergillosis. AFUEI is an inhibitor of the elastase derived from Aspergillus fumigatus. AFUEI is a member of the I78 inhibitor family and has a high inhibitory activity against elastases of Aspergillus fumigatus and Aspergillus flavus, human neutrophil elastase and bovine chymotrypsin, but does not inhibit bovine trypsin. Here we report ...
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Elastolytic and elastase inhibitory activities were investigated for 13 strains of Aspergillus fumigatus, three strains of Aspergillus flavus and three strains of Aspergillus niger. Nine of the 13 strains of A. fumigatus and all strains of A. flavus demonstrated elastase activity (more than 1 unit ml(-1)). Six of the 13 strains of A. fumigatus and all strains of A. flavus expressed elastase inh...
متن کاملCharacterization and primary structure of elastase inhibitor, AFLEI, from Aspergillus flavus.
The amino acid sequence of elastase inhibitor, AFLEI, isolated from Aspergillus flavus was determined by the Edman sequencing procedure of peptides derived from digests utilizing clostripain. A molecular weight of 7,525.8 was observed by TOF-MS. AFLEI contained 68 amino acid residues and has a calculated molecular weight of 7,526.2. The search for amino acid homology with other proteins demonst...
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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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ژورنال
عنوان ژورنال: Journal of Medical Microbiology
سال: 2008
ISSN: 0022-2615,1473-5644
DOI: 10.1099/jmm.0.47789-0