Studies on the high-sulphur proteins of reduced mohair. The isolation and amino acid sequence of protein scmkb-m1.2

Biochem J. 1975 Mar;145(3):459-67. doi: 10.1042/bj1450459.

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

  • Amino Acid Sequence
  • Animals
  • Chymotrypsin
  • Goats
  • Papain
  • Pepsin A
  • Peptide Fragments / analysis
  • Proteins / isolation & purification*
  • Sulfur / analysis*
  • Thermolysin
  • Trypsin
  • Wool / analysis*

Substances

  • Peptide Fragments
  • Proteins
  • Sulfur
  • Chymotrypsin
  • Trypsin
  • Papain
  • Pepsin A
  • Thermolysin