The carbohydrate moiety of the acid carboxypeptidase from Aspergillus saitoi

Acid carboxypeptidase from Aspergillus saitoi is a glycoprotein that contains both N- and O-linked sugar chains. The N-glycanase released high-mannose type oligosaccharides that were separated into eight components on HPLC. One, which had a unique structure of Man11GlcNAc2, was characterized. Mild a...

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Bibliographic Details
Published in:Current microbiology 1993-11, Vol.27 (5), p.281-288
Main Authors: Chiba, Y, Yamagata, Y, Iijima, S, Nakajima, T, Ichishima, E
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
ASPERGILLUS
Aspergillus - enzymology
Aspergillus saitoi
Biological and medical sciences
Biotechnology
CARBOHIDRATOS
Carbohydrate Sequence
Carbohydrates - chemistry
Carboxypeptidases - chemistry
Carboxypeptidases - drug effects
Carboxypeptidases - isolation & purification
Carboxypeptidases - secretion
Fundamental and applied biological sciences. Psychology
GLUCIDE
Growth, nutrition, metabolism, transports, enzymes. Molecular biology
Microbiology
Molecular Sequence Data
Mycology
Oligosaccharides - chemistry
PEPTIDASAS
PEPTIDASE
Tunicamycin - pharmacology
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Summary:Acid carboxypeptidase from Aspergillus saitoi is a glycoprotein that contains both N- and O-linked sugar chains. The N-glycanase released high-mannose type oligosaccharides that were separated into eight components on HPLC. One, which had a unique structure of Man11GlcNAc2, was characterized. Mild alkali treatment of the carboxypeptidase, under conditions that effect beta-elimination, yielded D-mannose. Deglycosylation of the carboxypeptidase with endo-beta-N-acetylglucosaminidase and alpha-mannosidase effected the reduction of the molecular mass from 72 kDa to 60 kDa. Partial changes of CD spectra of the native and the deglycosylated enzymes indicate that some conformational changes on the peptide of the enzyme occurred after deglycosylation. Other enzymatic properties, such as catalytic activity, pH, and thermal stability and resistivity to protease digestion, did not appear to change. Tunicamycin halted secretion of the carboxypeptidase extracellularly
ISSN:0343-8651
1432-0991
DOI:10.1007/BF01575993