Two glycosylation patterns for a single protein (exoglucanase) in Saccharomyces cerevisiae.
Exoglucanases (beta-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.
Ramírez
M
M
Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, Badajoz, Spain.
Muñoz
M D
MD
Basco
R D
RD
Giménez-Gallego
G
G
Hernández
L M
LM
Larriba
G
G
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D006031:Glycosylation; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D001617:beta-Glucosidase / Q000032:analysis / Q000378:metabolism*
D000596:Amino Acids; D001617:beta-Glucosidase