Covalent Structure of Collagen

Amino Acid Sequence of Five Consecutive CNBr Peptides from Type III Collagen of Human Liver†

Jerome M. Seyer, Andrew Kang

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Type III collagen was solubilized from human liver by limited pepsin digestion and purified by differential salt precipitation and carboxymethylcellulose chromatography. Digestion with cyanogen bromide yielded the nine distinct peptides previously described and an additional tripeptide not recognized in earlier studies. Five of these peptides, αl(III)-CB1,2,4, 8, and 10, were further purified by molecular sieve and/or ion exchange chromatography. They contained 12, 40, 149, 125 and 3 amino acid residues, respectively. The amino acid sequence of these peptides was determined by automated Edman degradation of tryptic (before and after maleylation), chymotryptic, thermolytic or hydroxylamine-derived peptide fragments as well as the intact peptides. The alignment of these five peptides within the collagen chain is deduced to be 1-810-2-4 by homology with known α 1(I) sequences. The known CNBr peptide alignment of the NH2-terminal portion of type III collagen so far would, therefore, be α1(III)-CB3-7-6-l-8-10-2-4 and correspond to the homologous region of α1(I)-CBO-1-2-4-5-8-3 or residues 11-567 of the α1 (III) collagen chain.

Original languageEnglish (US)
Pages (from-to)3404-3411
Number of pages8
JournalBiochemistry
Volume17
Issue number16
DOIs
StatePublished - Jan 1 1978

Fingerprint

Collagen Type III
Liver
Amino Acid Sequence
Collagen
Amino Acids
Peptides
Chromatography
Digestion
Cyanogen Bromide
Carboxymethylcellulose Sodium
Hydroxylamine
Peptide Fragments
Pepsin A
Molecular sieves
Ion Exchange Chromatography
Ion exchange
Salts
Degradation

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Covalent Structure of Collagen : Amino Acid Sequence of Five Consecutive CNBr Peptides from Type III Collagen of Human Liver†. / Seyer, Jerome M.; Kang, Andrew.

In: Biochemistry, Vol. 17, No. 16, 01.01.1978, p. 3404-3411.

Research output: Contribution to journalArticle

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abstract = "Type III collagen was solubilized from human liver by limited pepsin digestion and purified by differential salt precipitation and carboxymethylcellulose chromatography. Digestion with cyanogen bromide yielded the nine distinct peptides previously described and an additional tripeptide not recognized in earlier studies. Five of these peptides, αl(III)-CB1,2,4, 8, and 10, were further purified by molecular sieve and/or ion exchange chromatography. They contained 12, 40, 149, 125 and 3 amino acid residues, respectively. The amino acid sequence of these peptides was determined by automated Edman degradation of tryptic (before and after maleylation), chymotryptic, thermolytic or hydroxylamine-derived peptide fragments as well as the intact peptides. The alignment of these five peptides within the collagen chain is deduced to be 1-810-2-4 by homology with known α 1(I) sequences. The known CNBr peptide alignment of the NH2-terminal portion of type III collagen so far would, therefore, be α1(III)-CB3-7-6-l-8-10-2-4 and correspond to the homologous region of α1(I)-CBO-1-2-4-5-8-3 or residues 11-567 of the α1 (III) collagen chain.",
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AB - Type III collagen was solubilized from human liver by limited pepsin digestion and purified by differential salt precipitation and carboxymethylcellulose chromatography. Digestion with cyanogen bromide yielded the nine distinct peptides previously described and an additional tripeptide not recognized in earlier studies. Five of these peptides, αl(III)-CB1,2,4, 8, and 10, were further purified by molecular sieve and/or ion exchange chromatography. They contained 12, 40, 149, 125 and 3 amino acid residues, respectively. The amino acid sequence of these peptides was determined by automated Edman degradation of tryptic (before and after maleylation), chymotryptic, thermolytic or hydroxylamine-derived peptide fragments as well as the intact peptides. The alignment of these five peptides within the collagen chain is deduced to be 1-810-2-4 by homology with known α 1(I) sequences. The known CNBr peptide alignment of the NH2-terminal portion of type III collagen so far would, therefore, be α1(III)-CB3-7-6-l-8-10-2-4 and correspond to the homologous region of α1(I)-CBO-1-2-4-5-8-3 or residues 11-567 of the α1 (III) collagen chain.

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