Purification of the inducible α‐agglutinin of S. cerevisiae and molecular cloning of the gene

FEBS Letters

Hauser, Karin¹  Tanner, Widmar¹ 

[1] Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universität Regensburg, 8400 Regensburg, FRG

关键词: Agglutinin;    α-;    Glycoprotein;    DNA sequence;    (Saccharomyces cerevisiae);   

DOI  :  10.1016/0014-5793(89)81108-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The α-agglutinin responsible for mating type-specific agglutination of S. cerevisiae α-cells has been purified to homogeneity. The glycoprotein released from the cell surface under mild conditions has a relative molecular mass of 200 to 300 kDa as determined by SDS-gel electrophoresis. The protein moiety corresponds to 68.2 kDa. With an oligonucleotide corresponding to the N-terminal amino acid sequence, the α-agglutinin gene has been cloned and sequenced. From the DNA sequence, a protein of 631 amino acids with 12 potential N-glycosylation sites is predicted. The carboxy terminal one-third of the protein is not required for agglutination activity.

【 授权许可】

Unknown