title: [Isoelectric focusing of a preparation of proteolytic enzymes from Streptomyces 771].
abstract: The proteolytic enzymes contained in the preparation from Streptomyces 771 have been separated by isoelectric focusing in the sucrose density gradient at pH 3-10. The following enzymes have been identified: three multiple forms of neutral metal proteinase (pI 5.1, 6.37, 7.8) each of which splits DNP-Gly-Gly decreases-Val-ArgOMe; elastase-like metal proteinase active with respect to RBB-elestin with pI 10.68; metal-dependent peptidases: leucin aminopeptidase active with respect to L-RBB-elastin with pI 10.68 metal-dependent peptidases: leucin aminopeptidase active with respect to L-leucin n-nitroanilide and L-leucin beta-naphtylamide with pI 7.65, 7.15, 6.67, 6.45, 5.7, 5.35, 5.22, 4.83; carboxy peptidase with pI 5.95, 6.37; serine metal-dependent subtilisin-like proteinase active with respect to 2-Ala-Ala-LeupNA, 2-Gly-Gly-LeupNA, 2-Ala-LeupNA; two multiple forms of serine trypsin-like proteinase active with respect to BAEE and BApNA with pI 4.35, 4.76; serine chymotrypsin-like proteinase with pI 8.68 active with respect to ATEE.
mesh_terms: D007525:Isoelectric Focusing / Q000379:methods; D010447:Peptide Hydrolases / Q000032:analysis* / Q000302:isolation & purification; D013056:Spectrophotometry, Ultraviolet; D013302:Streptomyces / Q000201:enzymology*
chemical_list: D010447:Peptide Hydrolases
vernacular_title: Izoélektricheskoe fokusirovanie preparata proteoliticheskikh fermentov iz Streptomyces 771.