Covalent Structure of Collagen

Amino Acid Sequence of al(III)-CB9 from Type III Collagen of Human Liver

Jerome M. Seyer, Andrew Kang

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

The peptide al(III)-CB9 was prepared and purified from human liver, and its amino acid sequence was determined. Automated Edman degradation of the intact peptide and peptides derived from selective cleavage with hydroxylamine and digestions with trypsin, thermolysin, and Staph V8 protease enabled determination of the complete amino acid sequence. The peptide al(III)-CB9 represents the COOH terminus of the helical (pepsin-resistant) portion of type III collagen and terminates in a Cys-Cys sequence responsible for the intramolecular disulfide cross-linkages with other chains. The present work completes the entire amino acid sequence of the helical (pepsin-resistant) portion of human cirrhotic liver type III collagen consisting of peptides α1-(III)-CB3-7-6-1 -8-10-2-4-5-9. The COOH terminus of human liver al(III) contained two additional triplets which, together with the extra triplet at the NH2 terminus in al(III)-CB3, make the helical portion of type III collagen longer than a 1(1) by nine residues (three Gly-X-Y triplets). The helical region of human liver type III collagen, therefore, consists of 1023 amino acids or 341 triplets.

Original languageEnglish (US)
Pages (from-to)2621-2627
Number of pages7
JournalBiochemistry
Volume20
Issue number9
DOIs
StatePublished - Jan 1 1981

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Collagen Type III
Liver
Amino Acid Sequence
Collagen
Amino Acids
Peptides
Pepsin A
cysteinylcysteine
Thermolysin
Hydroxylamine
Protein Sequence Analysis
Disulfides
Trypsin
Digestion
Degradation

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Covalent Structure of Collagen : Amino Acid Sequence of al(III)-CB9 from Type III Collagen of Human Liver. / Seyer, Jerome M.; Kang, Andrew.

In: Biochemistry, Vol. 20, No. 9, 01.01.1981, p. 2621-2627.

Research output: Contribution to journalArticle

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title = "Covalent Structure of Collagen: Amino Acid Sequence of al(III)-CB9 from Type III Collagen of Human Liver",
abstract = "The peptide al(III)-CB9 was prepared and purified from human liver, and its amino acid sequence was determined. Automated Edman degradation of the intact peptide and peptides derived from selective cleavage with hydroxylamine and digestions with trypsin, thermolysin, and Staph V8 protease enabled determination of the complete amino acid sequence. The peptide al(III)-CB9 represents the COOH terminus of the helical (pepsin-resistant) portion of type III collagen and terminates in a Cys-Cys sequence responsible for the intramolecular disulfide cross-linkages with other chains. The present work completes the entire amino acid sequence of the helical (pepsin-resistant) portion of human cirrhotic liver type III collagen consisting of peptides α1-(III)-CB3-7-6-1 -8-10-2-4-5-9. The COOH terminus of human liver al(III) contained two additional triplets which, together with the extra triplet at the NH2 terminus in al(III)-CB3, make the helical portion of type III collagen longer than a 1(1) by nine residues (three Gly-X-Y triplets). The helical region of human liver type III collagen, therefore, consists of 1023 amino acids or 341 triplets.",
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N2 - The peptide al(III)-CB9 was prepared and purified from human liver, and its amino acid sequence was determined. Automated Edman degradation of the intact peptide and peptides derived from selective cleavage with hydroxylamine and digestions with trypsin, thermolysin, and Staph V8 protease enabled determination of the complete amino acid sequence. The peptide al(III)-CB9 represents the COOH terminus of the helical (pepsin-resistant) portion of type III collagen and terminates in a Cys-Cys sequence responsible for the intramolecular disulfide cross-linkages with other chains. The present work completes the entire amino acid sequence of the helical (pepsin-resistant) portion of human cirrhotic liver type III collagen consisting of peptides α1-(III)-CB3-7-6-1 -8-10-2-4-5-9. The COOH terminus of human liver al(III) contained two additional triplets which, together with the extra triplet at the NH2 terminus in al(III)-CB3, make the helical portion of type III collagen longer than a 1(1) by nine residues (three Gly-X-Y triplets). The helical region of human liver type III collagen, therefore, consists of 1023 amino acids or 341 triplets.

AB - The peptide al(III)-CB9 was prepared and purified from human liver, and its amino acid sequence was determined. Automated Edman degradation of the intact peptide and peptides derived from selective cleavage with hydroxylamine and digestions with trypsin, thermolysin, and Staph V8 protease enabled determination of the complete amino acid sequence. The peptide al(III)-CB9 represents the COOH terminus of the helical (pepsin-resistant) portion of type III collagen and terminates in a Cys-Cys sequence responsible for the intramolecular disulfide cross-linkages with other chains. The present work completes the entire amino acid sequence of the helical (pepsin-resistant) portion of human cirrhotic liver type III collagen consisting of peptides α1-(III)-CB3-7-6-1 -8-10-2-4-5-9. The COOH terminus of human liver al(III) contained two additional triplets which, together with the extra triplet at the NH2 terminus in al(III)-CB3, make the helical portion of type III collagen longer than a 1(1) by nine residues (three Gly-X-Y triplets). The helical region of human liver type III collagen, therefore, consists of 1023 amino acids or 341 triplets.

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