title: Studies on the high-sulphur proteins of reduced mohair. The isolation and amino acid sequence of protein scmkb-m1.2.
abstract: The complete amino acid sequence of mohair protein, SCMKB-M1.2 (97 residues), was determined. The protein was isolated from reduced and carboxymethylated mohair by chromatography on DEAE-cellulose phosphate. Peptides for sequence determination were obtained by digestion with trypsin, pepsin, chymotrypsin, thermolysin and papain, and were fractionated by DEAE-cellulose chromatography, paper chromatography and electrophoresis. The sequence of the peptides were determined by the Edman degradation method (by use of both the Beckman Sequence and a non-automatic procedure), and by partial acid hydrolysis. The protein is closely homologous to wool protein SCMKB-IIIB2, and also contains acetylated alanine as N-terminal amino acid.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002918:Chymotrypsin; D006041:Goats; D010206:Papain; D010434:Pepsin A; D010446:Peptide Fragments / Q000032:analysis; D011506:Proteins / Q000302:isolation & purification*; D013455:Sulfur / Q000032:analysis*; D013820:Thermolysin; D014357:Trypsin; D014935:Wool / Q000032:analysis*
chemical_list: D010446:Peptide Fragments; D011506:Proteins; D013455:Sulfur; D002918:Chymotrypsin; D014357:Trypsin; D010206:Papain; D010434:Pepsin A; D013820:Thermolysin