[Primary structure of intracellular serine proteinase from Bacillus amyloliquefaciens. I. Isolation of the enzyme and amino acid sequence of peptides of tryptic hydrolysate].
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.
Surova
I A
IA
Ianonis
V V
VV
Revina
L P
LP
Levin
E D
ED
Stepanov
V M
VM
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D006868:Hydrolysis; D012697:Serine Endopeptidases / Q000032:analysis / Q000302:isolation & purification*; D014357:Trypsin
D012697:Serine Endopeptidases; D014357:Trypsin
Pervichnaia struktura vnutrikletochnoĭ serinovoĭ proteinazy Bacillus amyloliquefaciens. I. Vydelenie fermenta i opredelenie aminokislotnoĭ posledovatel'nosti peptidov tripticheskogo gidrolizata.