A number of cell surface glycoproteins can be specifically and completely released from intact cells of Saccharomyces cerevisiae with 0.5% mercaptoethanol. Among these proteins is one with a molecular mass of 22 kDa, which is synthesized only in haploid a cells treated with the peptide mating pheromone α factor. This protein could be radiolabeled in vivo with [2-3H]mannose, [14C]phenylaline, and [35S]sulfate. Its synthesis and export to the cell surface were not inhibited by tunicamycin. β-Elimination released almost all radioactivity from the [2-3H]mannose-labeled protein, 36% of its radioactivity being recovered subsequently as mannose and 43% as a dimannoside. Evidence is presented that the 22-kDa O-glycosylated protein is a mating-specific a cell agglutinin.
|Original language||English (US)|
|Number of pages||4|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - 1986|
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