---

Terrance K, et al.  (1987) Identification of glycoprotein components of alpha-agglutinin, a cell adhesion protein from Saccharomyces cerevisiae. J Bacteriol 169(2):475-82

Abstract: Several glycoproteins which inhibit the agglutinability of Saccharomyces cerevisiae mating type a cells were partially purified from extracts of mating type alpha cells. These proteins, called alpha-agglutinin, were labeled with 125I-Bolton-Hunter reagent. The labeled alpha-agglutinin showed specific binding to a cells. Such specific binding approached saturation with respect to agglutinin or cells and was inhibited in the presence of excess unlabeled alpha-agglutinin. Nonspecific binding was similar in a and alpha cells, was neither saturable nor competable, and was three- to fourfold less than the specific binding to a cells at maximum tested agglutinin concentrations. The major a-specific binding species had a low electrophoretic mobility in sodium dodecyl sulfate-polyacrylamide gels and had an apparent molecular weight of 155,000 by rate zonal centrifugation. Endo-N-acetylglucosaminidase H digestion of the purified glycoprotein complex converted the low-mobility material to four major and several minor bands which were resolved by polyacrylamide gel electrophoresis. All but two minor peptides bound specifically to a cells. Analyses of agglutinin from mnn mutants confirmed the deglycosylation results in suggesting that the N-linked carbohydrate portion of alpha-agglutinin was not necessary for activity.

Status: Published

Type: Journal Article

PubMed ID: 3542959

---

Author Searches

To find contact information or other publications by the authors of this paper, follow these three steps:

1. (1) Choose an author,
2. (2) Choose a search parameter,
3. (3) Click to implement

Terrance K Heller P Wu YS Lipke PN Papers in SGD Colleagues in SGD PubMed Google Scholar

---