Covalent Structure of Collagen

Amino Acid Sequence of α 1(III)-CB5 from Type III Collagen of Human Liver

Jerome M. Seyer, Carlo Mainardi, Andrew Kang

Research output: Contribution to journalArticle

21 Citations (Scopus)

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 αl(III)-CB5 was further purified by carboxymethylcellulose chromatography, and its amino acid sequence was determined. Automatic Edman degradation of intact αl(III)-CB5, tryptic and thermolytic peptides, and hydroxylamine-derived fragments was used to establish the total sequence. the mammalian collagenase site contained in the αl(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 αl(III)-CB3-7-6-l-8-10-2-4-5. These correspond to the homologous region of αl(I)-CB0-l-2-4-5-8-3-7 residues 11-804.

Original languageEnglish (US)
Pages (from-to)1583-1589
Number of pages7
JournalBiochemistry
Volume19
Issue number8
DOIs
StatePublished - Feb 1 1980

Fingerprint

Collagen Type III
Collagenases
Liver
Digestion
Amino Acid Sequence
Carboxymethylcellulose Sodium
Collagen
Chromatography
Amino Acids
Peptides
Cyanogen Bromide
Hydroxylamine
Pepsin A
Collagen Type I
Salts
Degradation

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Covalent Structure of Collagen : Amino Acid Sequence of α 1(III)-CB5 from Type III Collagen of Human Liver. / Seyer, Jerome M.; Mainardi, Carlo; Kang, Andrew.

In: Biochemistry, Vol. 19, No. 8, 01.02.1980, p. 1583-1589.

Research output: Contribution to journalArticle

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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 αl(III)-CB5 was further purified by carboxymethylcellulose chromatography, and its amino acid sequence was determined. Automatic Edman degradation of intact αl(III)-CB5, tryptic and thermolytic peptides, and hydroxylamine-derived fragments was used to establish the total sequence. the mammalian collagenase site contained in the αl(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 αl(III)-CB3-7-6-l-8-10-2-4-5. These correspond to the homologous region of αl(I)-CB0-l-2-4-5-8-3-7 residues 11-804.",
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N2 - 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 αl(III)-CB5 was further purified by carboxymethylcellulose chromatography, and its amino acid sequence was determined. Automatic Edman degradation of intact αl(III)-CB5, tryptic and thermolytic peptides, and hydroxylamine-derived fragments was used to establish the total sequence. the mammalian collagenase site contained in the αl(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 αl(III)-CB3-7-6-l-8-10-2-4-5. These correspond to the homologous region of αl(I)-CB0-l-2-4-5-8-3-7 residues 11-804.

AB - 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 αl(III)-CB5 was further purified by carboxymethylcellulose chromatography, and its amino acid sequence was determined. Automatic Edman degradation of intact αl(III)-CB5, tryptic and thermolytic peptides, and hydroxylamine-derived fragments was used to establish the total sequence. the mammalian collagenase site contained in the αl(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 αl(III)-CB3-7-6-l-8-10-2-4-5. These correspond to the homologous region of αl(I)-CB0-l-2-4-5-8-3-7 residues 11-804.

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