title: Purification and amino acid sequence of mating factor from Saccharomyces cerevisiae.
abstract: Mating factor is a peptide excreted into the culture fluid by alpha-mating type cells of Saccharomyces cerevisiae X-2180 1B. The purification of the mating factor was carried out by ion exchange chromatography on phosphocellulose and Amberlite IRC 50 columns, followed by gel filtration on a Sephadex LH 20 column. The factor thus prepared was a peptide composed of Lys1, His1, Trp2, Gln2, Pro2, Gly1, Met1, Leu2 and Tyr1, and was able to induce morphological changes on alpha-mating type cells at a concentration of 5 pg/ml. The amino acid sequence of the mating factor was determined by the manual Edman degradation method using intact mating factor and its thermolytic peptides. The C-terminal amino acid residue was determined by digesting the factor with carboxypeptidase A. The complete amino acid sequence of the mating factor was established to be as follows: Trp-His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr.
mesh_terms: D000595:Amino Acid Sequence; D010446:Peptide Fragments / Q000032:analysis; D010455:Peptides / Q000302:isolation & purification / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000502:physiology*; D013056:Spectrophotometry, Ultraviolet
chemical_list: D010446:Peptide Fragments; D010455:Peptides