[Primary structure of an intracellular serine proteinase from Bacillus amyloliquefaciens. II. Amino acid sequence of peptides in a chymotrypsin hydrolysate].

Autor: Surova IA, Ianonis VV, Revina LP, Ostoslavskaia VI, Kolesnikova LA, Timokhina EA, Levin ED, Stepanov VM
Jazyk: ruština
Zdroj: Bioorganicheskaia khimiia [Bioorg Khim] 1994 Apr; Vol. 20 (4), pp. 382-92.
Abstrakt: Chymotrypsin hydrolyzate of the intracellular serine protease was separated by ion-exchange chromatography on a sulphocationite resin followed by HPLC to yield fifty one individual peptides. Their sequences, corresponding in total to 381 amino acid residues, were determined by the manual Edman procedure.
Databáze: MEDLINE