title: [Primary structure of intracellular serine proteinase from Bacillus amyloliquefaciens. I. Isolation of the enzyme and amino acid sequence of peptides of tryptic hydrolysate].
abstract: Method of isolation of intracellular serine protease was modified. Gramicidin S-sepharose CL-4B with a higher content of the ligand, synthesized through a modified procedure, was used as an affinity sorbent which simplified the purification and led to the pure enzyme with high specific activity and 90% yield. Trypsin hydrolyzate of the protease was separated by ion-exchange chromatography on a sulphocationite resin followed by paper chromatography and paper electrophoresis to yield twenty-five individual peptides. Their complete or partial sequences, corresponding in total to 146 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: 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*; D006868:Hydrolysis; D012697:Serine Endopeptidases / Q000032:analysis / Q000302:isolation & purification*; D014357:Trypsin
chemical_list: D012697:Serine Endopeptidases; D014357:Trypsin
vernacular_title: Pervichnaia struktura vnutrikletochnoĭ serinovoĭ proteinazy Bacillus amyloliquefaciens. I. Vydelenie fermenta i opredelenie aminokislotnoĭ posledovatel'nosti peptidov tripticheskogo gidrolizata.