Open AccessTwo glycosylation patterns for a single protein (exoglucanase) in Saccharomyces cerevisiae
Author(s) -
Ra'irez Manuel,
Dolores Muñoz M.,
Basco Ricardo D.,
GiménezGallego Guillermo,
Hernández Luis M.,
Larriba Germán
Publication year - 1990
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.1574-6968.1990.tb03796.x
Subject(s) - saccharomyces cerevisiae , glycosylation , biochemistry , chemistry , biology , yeast
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 NH 2 ‐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.