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Glycobiology Advance Access published online on May 5, 2004
Glycobiology, doi:10.1093/glycob/cwh091
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Received October 13, 2003
Revised January 8, 2004
Accepted January 9, 2004

ORIGINAL ARTICLES

Hydrolysis of Man9GlcNAc2 and Man8GlcNAc2 oligosaccharides by a purified {alpha}-mannosidase from Candida albicans

Héctor M. Mora-Montes 1, Everardo López-Romero 1, Samuel Zinker 2, Patricia Ponce-Noyola 1, Arturo Flores-Carreón 1*

1 Instituto de Investigación en Biología Experimental, Facultad de Química, Universidad de Guanajuato, Guanajuato, Guanajuato 36000, México
2 Departamento de Genética y Biología Molecular, CINVESTAV del IPN, Apartado Postal 14-740, México, D.F. 07000, México

* To whom correspondence should be addressed. E-mail: floresca{at}quijote.ugto.mx.


  Abstract

A soluble {alpha}-mannosidase from Candida albicans was purified to homogeneity by sequential size exclusion, ion exchange and affinity chromatographies in columns of Sepharose CL6B, DEAE Bio-Gel A and Concanavalin A Sepharose 4B, respectively. Analytical electrophoresis of the purified preparation in 10% SDS-polyacrylamide gels stained with Coomassie Blue revealed a single polypeptide of 43 kDa that was responsible for enzyme activity. The purified enzyme primarily trimmed Man9GlcNAc2 to produce Man8GlcNAc2 isomer B and mannose as a function of time of incubation up to 12 h at 37°C. Prolonged incubation with the enzyme resulted in the accumulation after 24 h of other oligosaccharides corresponding to Man7GlcNAc2 and probably Man6GlcNAc2. These two products were also observed when Man8GlcNAc2 isomer B instead of Man9GlcNAc2 was used as substrate. Other oligosaccharides such as Man6GlcNAc2-Asn and Man5GlcNAc2-Asn and the {alpha}1,3- and {alpha}1,6-linked mannobiosides were not hydrolyzed at all. These properties are consistent with an {alpha}1,2-mannosidase that may represent a new member of the glycosylhydrolase family 47.

Key words: Candida albicans, {alpha}1,2-mannosidase, protein N-glycosylation


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