title: Covalent structure of collagen: amino acid sequence of alpha 1 (III)-CB5 from type III collagen of human liver.
abstract: Type III collagen was prepared from human liver by limited pepsin digestion, differential salt precipitation, and carboxymethylcellulose chromatography. Ten distinct peptides were obtained by cyanogen bromide digestion. The peptide alpha 1 (III)-CB5 was further purified by carboxymethylcellulose chromatography, and its amino acid sequence was determined. Automatic Edman degradation of intact alpha 1 (III)-CB5, tryptic and thermolytic peptides, and hydroxylamine-derived fragments was used to establish the total sequence. The mammalian collagenase site contained in the alpha 1 (III)-CB5 sequence was ascertained by digestion of native type III collagen with purified rheumatoid synovial collagenase. Collagenase cleavage occurred at a single Gly--Ile bond, one triplet before the corresponding specific cleavage site of type I collagen. The present work brings the known sequence of human liver type III collagen to include alpha 1 (III)-CB3-7-6-1-8-10-2-4-5. These correspond to the homologous region of alpha 1 (I)-CB0-1-2-4-5-8-3-7 residues 11--804.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003094:Collagen; D006801:Humans; D008099:Liver / Q000032:analysis*; D008103:Liver Cirrhosis / Q000378:metabolism; D003012:Microbial Collagenase; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity; D014357:Trypsin
chemical_list: D010446:Peptide Fragments; D003094:Collagen; D014357:Trypsin; D003012:Microbial Collagenase