Open AccessPurification of soluble α1,2‐mannosidase from Candida albicans CAI‐4
Author(s) -
MoraMontes Héctor M.,
LópezRomero Everardo,
Zinker Samuel,
PonceNoyola Patricia,
FloresCarreón Arturo
Publication year - 2006
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.1574-6968.2006.00093.x
Subject(s) - mannosidase , endoplasmic reticulum , enzyme , mannose , biochemistry , glycoside hydrolase , hydrolase , chemistry , candida albicans , specific activity , biology , microbiology and biotechnology
A soluble α‐mannosidase from Candida albicans CAI‐4 was purified by conventional methods of protein isolation. Analytical electrophoresis of the purified preparation revealed two polypeptides of 52 and 27 kDa, the former being responsible for enzyme activity. The purified, 52 kDa enzyme trimmed Man 9 GlcNAc 2 , producing Man 8 GlcNAc 2 isomer B and mannose, and was inhibited preferentially by 1‐deoxymannojirimycin. These properties are consistent with an endoplasmic reticulum‐resident α1,2‐mannosidase of the glycosyl hydrolase family 47. Moreover, a proteolytic activity responsible for converting the 52 kDa α‐mannosidase into a polypeptide of 43 kDa retaining full enzyme activity, was demonstrated in membranes of ATCC 26555, but not in CAI‐4 strain.