Two glycosylation patterns for a single protein (exoglucanase) in Saccharomyces cerevisiae

Exoglucanases (β‐glucosidases) I and II secreted into the culture medium by Saccharomyces cerevisiae were purified from cell cultures harvested at the early exponential phase of growth in order to avoid contamination of the second by a new immunologically‐related material. The amino acid composition...

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Bibliographic Details
Published in:FEMS microbiology letters 1990-09, Vol.71 (1‐2), p.43-48
Main Authors: Ra'irez, Manuel, Dolores Muñoz, M., Basco, Ricardo D., Giménez‐Gallego, Guillermo, Hernández, Luis M., Larriba, Germán
Format: Article
Language:English
Subjects:
amino acid composition
amino acid sequence
Amino terminal sequence
beta -glucosidase
beta -glucosidase II
Carbohydrate modification
Exoglucanase (β‐glucosidase)
extracellular enzymes
glycosylation
Morphogenesis
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Summary:Exoglucanases (β‐glucosidases) I and II secreted into the culture medium by Saccharomyces cerevisiae were purified from cell cultures harvested at the early exponential phase of growth in order to avoid contamination of the second by a new immunologically‐related material. The amino acid composition of the purified enzymes was roughly the same. In addition, both exoglucanases exhibited an identical NH2‐terminal sequence (50 residues). These results confirm our previous results about the identity of the protein moieties of both enzymes. Exoglucanase I appears to arise by elongation of one or both short oligosaccharides present in enzyme II.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1990.tb03796.x