title: [Primary structure of an intracellular serine proteinase from Bacillus amyloliquefaciens. II. Amino acid sequence of peptides in a chymotrypsin hydrolysate].
abstract: 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.
authors.forename: I A
authors.initials: IA
authors.lastname: Surova
authors.forename: V V
authors.initials: VV
authors.lastname: Ianonis
authors.forename: L P
authors.initials: LP
authors.lastname: Revina
authors.forename: V I
authors.initials: VI
authors.lastname: Ostoslavskaia
authors.forename: L A
authors.initials: LA
authors.lastname: Kolesnikova
authors.forename: E A
authors.initials: EA
authors.lastname: Timokhina
authors.forename: E D
authors.initials: ED
authors.lastname: Levin
authors.forename: V M
authors.initials: VM
authors.lastname: Stepanov
mesh_terms: D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D002918:Chymotrypsin; D006868:Hydrolysis; D010449:Peptide Mapping; D012697:Serine Endopeptidases / Q000737:chemistry*
chemical_list: D012697:Serine Endopeptidases; D002918:Chymotrypsin
vernacular_title: Pervichnaia struktura vnutrikletochnoĭ serinovoĭ proteinazy Bacillus amyloliquefaciens. II. Aminokislotnaia posledovatel'nost' peptidov khimotripticheskogo gidrolizata.