| Title: | Purification of the inducible alpha-agglutinin of S. cerevisiae and molecular cloning of the gene |
| Address: | "Lehrstuhl fur Zellbiologie und Pflanzenphysiologie, Universitat Regensburg, FRG" |
| DOI: | 10.1016/0014-5793(89)81108-1 |
| ISSN/ISBN: | 0014-5793 (Print) 0014-5793 (Linking) |
| Abstract: | "The alpha-agglutinin responsible for mating type-specific agglutination of S. cerevisiae alpha-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 alpha-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" |
| Keywords: | "Agglutination Amino Acid Sequence Base Sequence *Cloning, Molecular *Genes, Fungal Mating Factor Molecular Sequence Data Peptide Biosynthesis Peptides/genetics/*isolation & purification Pheromones/isolation & purification Saccharomyces cerevisiae/*genetic;" |
| Notes: | "MedlineHauser, K Tanner, W eng England 1989/09/25 FEBS Lett. 1989 Sep 25; 255(2):290-4. doi: 10.1016/0014-5793(89)81108-1" |
