Evidence of homology in a high-sulphur protein fraction (SCMK-B2) of wool and hair alpha-keratins.
Fractions corresponding to the S-carboxymethylated high-sulphur protein component SCMK-B2 isolated by Gillespie (1963) from Merino wool were prepared from five different wool samples and also from bovine hair. The six fractions showed great similarities in amino acid composition, and also gave very similar peptide ;maps' after tryptic and chymotryptic digestion. Some of the peptides were isolated from the different samples, and evidence is given that suggests that a sequence of at least 21 amino acids is common to all the fraction SCMK-B2 preparations. Further, all the fractions derived from the wool samples have the same acetylated heptapeptide for the N-terminal sequence, but one extra residue may be present in this N-terminal sequence in the protein from bovine hair. The general significance of these findings is discussed.
D000818:Animals; D002417:Cattle; D002918:Chymotrypsin / Q000494:pharmacology; D004586:Electrophoresis; D006197:Hair / Q000032:analysis*; D007633:Keratins / Q000032:analysis*; D012756:Sheep; D013455:Sulfur / Q000032:analysis; D014357:Trypsin / Q000494:pharmacology; D014935:Wool / Q000032:analysis*
D007633:Keratins; D013455:Sulfur; D002918:Chymotrypsin; D014357:Trypsin