[Primary structure of an intracellular serine proteinase from Bacillus amyloliquefaciens. II. Amino acid sequence of peptides in a chymotrypsin hydrolysate].
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.
Surova
I A
IA
Ianonis
V V
VV
Revina
L P
LP
Ostoslavskaia
V I
VI
Kolesnikova
L A
LA
Timokhina
E A
EA
Levin
E D
ED
Stepanov
V M
VM
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*
D012697:Serine Endopeptidases; D002918:Chymotrypsin
Pervichnaia struktura vnutrikletochnoĭ serinovoĭ proteinazy Bacillus amyloliquefaciens. II. Aminokislotnaia posledovatel'nost' peptidov khimotripticheskogo gidrolizata.