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Primary structure of aspergillo pepsin a a carboxylic proteinase from aspergillus awamori 2. amino acid sequences of chymotryptic peptides


Soviet Journal of Bioorganic Chemistry 7(1): 47-55
Primary structure of aspergillo pepsin a a carboxylic proteinase from aspergillus awamori 2. amino acid sequences of chymotryptic peptides
Reduced and carboxymethylated aspergillopepsin A was hydrolyzed with chymotrypsin (100:1 substrate-enzyme ratio) at pH 8.0 and 37.degree. C. Soluble peptides were separated by ion-exchange chromatography on a sulfopolystyrene resin (chromobeads) using a gradient of pyridine-acetate buffer. Additional purification by paper chromatography or paper electrophoresis gave 30 peptides, which were analyzed by manual Edman procedure. Analysis of chymotryptic peptides elucidated the sequence of 57 amino acid residues. These data, along with those on tryptic peptides and sequencing of the enzyme N-terminal region, gave information on the sequence of, in total, 236 amino acid residues.


Accession: 006184808



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