Open AccessIdentification of precursor peptide of aculeacin A acylase as a protein with proteolytic activity
Author(s) -
Inokoshi J.,
Takeshima H.,
Omura S.
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06590.x
Subject(s) - molecular mass , antiserum , size exclusion chromatography , biochemistry , chemistry , peptide , incubation , proteolytic enzymes , enzyme , chromatography , biology , antigen , genetics
A protein with the proteolytic activity was isolated from culture filtrate of the aculeacin A acylase producing strain, Actinoplanes utahensis NRRL12052. The purified protein showed a single band of molecular mass of 87 kDa in SDS‐PAGE and gel filtration using HPLC, and reacted with anti‐aculeacin A acylase antiserum. The 87‐kDa protein was degraded to two peptides of molecular mass of 60 kDa and 19 kDa by incubation at 37°C in the presence of 0.1% SDS and the former band also responded to the antiserum. These results indicate that the 87‐kDa protein possessing the proteolytic activity is a precursor of aculeacin A acylase.