Covalent Structure of Collagen

Amino Acid Sequence of Cyanogen Bromide Peptides from the Amino-Terminal Segment of Type III Collagen of Human Liver

Jerome M. Seyer, Andrew Kang

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Human liver type III collagen was prepared by limited pepsin digestion, differential salt precipitation, and carboxymethylcellulose chromatography. Cyanogen bromide digestion of purified type III collagen chains yielded nine distinct peptides. Three peptides, α1(III)-CB3, α1(III)-CB7, and α1(III)-CB6, were isolated by carboxymethylcellulose chromatography and Sephadex G-50 SF gel filtration. Automated Edman degradation together with selective hydroxylamine cleavage and chymotrypsin and trypsin digestion enabled determination of their complete amino acid sequence. Compared with type I collagen, the data show tentative homology of α1(III)-CB3 with α1(I)-CBl, α1(I)-CB2, and α1(I)-CB4; al(III)-CB7 with α1(I)-CB5; and α1(III)-CB6 with the amino-terminal portion of α1(I)-CB8. Close interspecies homology was found between the sequences presented here with 90 residues of α1(III)-CB3 and 26 of α1(III)-CB8 of calf aorta. The present study establishes the amino acid sequence of 229 residues near the amino terminus or nearly one-quarter of the type III collagen chains. The disaccharide, Glc-Gal, was convalently bound to hydroxylysine at a position corresponding to the same location in the a 1(1) chain.

Original languageEnglish (US)
Pages (from-to)1158-1164
Number of pages7
JournalBiochemistry
Volume16
Issue number6
DOIs
StatePublished - Mar 1 1977

Fingerprint

Cyanogen Bromide
Collagen Type III
Liver
Digestion
Amino Acid Sequence
Carboxymethylcellulose Sodium
Collagen
Chromatography
Amino Acids
Peptides
Hydroxylysine
Hydroxylamine
Disaccharides
Pepsin A
Collagen Type I
Gel Chromatography
Aorta
Salts
Gels
Degradation

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Covalent Structure of Collagen : Amino Acid Sequence of Cyanogen Bromide Peptides from the Amino-Terminal Segment of Type III Collagen of Human Liver. / Seyer, Jerome M.; Kang, Andrew.

In: Biochemistry, Vol. 16, No. 6, 01.03.1977, p. 1158-1164.

Research output: Contribution to journalArticle

@article{ab896ad7536c457392f130cc9986597e,
title = "Covalent Structure of Collagen: Amino Acid Sequence of Cyanogen Bromide Peptides from the Amino-Terminal Segment of Type III Collagen of Human Liver",
abstract = "Human liver type III collagen was prepared by limited pepsin digestion, differential salt precipitation, and carboxymethylcellulose chromatography. Cyanogen bromide digestion of purified type III collagen chains yielded nine distinct peptides. Three peptides, α1(III)-CB3, α1(III)-CB7, and α1(III)-CB6, were isolated by carboxymethylcellulose chromatography and Sephadex G-50 SF gel filtration. Automated Edman degradation together with selective hydroxylamine cleavage and chymotrypsin and trypsin digestion enabled determination of their complete amino acid sequence. Compared with type I collagen, the data show tentative homology of α1(III)-CB3 with α1(I)-CBl, α1(I)-CB2, and α1(I)-CB4; al(III)-CB7 with α1(I)-CB5; and α1(III)-CB6 with the amino-terminal portion of α1(I)-CB8. Close interspecies homology was found between the sequences presented here with 90 residues of α1(III)-CB3 and 26 of α1(III)-CB8 of calf aorta. The present study establishes the amino acid sequence of 229 residues near the amino terminus or nearly one-quarter of the type III collagen chains. The disaccharide, Glc-Gal, was convalently bound to hydroxylysine at a position corresponding to the same location in the a 1(1) chain.",
author = "Seyer, {Jerome M.} and Andrew Kang",
year = "1977",
month = "3",
day = "1",
doi = "10.1021/bi00625a020",
language = "English (US)",
volume = "16",
pages = "1158--1164",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "6",

}

TY - JOUR

T1 - Covalent Structure of Collagen

T2 - Amino Acid Sequence of Cyanogen Bromide Peptides from the Amino-Terminal Segment of Type III Collagen of Human Liver

AU - Seyer, Jerome M.

AU - Kang, Andrew

PY - 1977/3/1

Y1 - 1977/3/1

N2 - Human liver type III collagen was prepared by limited pepsin digestion, differential salt precipitation, and carboxymethylcellulose chromatography. Cyanogen bromide digestion of purified type III collagen chains yielded nine distinct peptides. Three peptides, α1(III)-CB3, α1(III)-CB7, and α1(III)-CB6, were isolated by carboxymethylcellulose chromatography and Sephadex G-50 SF gel filtration. Automated Edman degradation together with selective hydroxylamine cleavage and chymotrypsin and trypsin digestion enabled determination of their complete amino acid sequence. Compared with type I collagen, the data show tentative homology of α1(III)-CB3 with α1(I)-CBl, α1(I)-CB2, and α1(I)-CB4; al(III)-CB7 with α1(I)-CB5; and α1(III)-CB6 with the amino-terminal portion of α1(I)-CB8. Close interspecies homology was found between the sequences presented here with 90 residues of α1(III)-CB3 and 26 of α1(III)-CB8 of calf aorta. The present study establishes the amino acid sequence of 229 residues near the amino terminus or nearly one-quarter of the type III collagen chains. The disaccharide, Glc-Gal, was convalently bound to hydroxylysine at a position corresponding to the same location in the a 1(1) chain.

AB - Human liver type III collagen was prepared by limited pepsin digestion, differential salt precipitation, and carboxymethylcellulose chromatography. Cyanogen bromide digestion of purified type III collagen chains yielded nine distinct peptides. Three peptides, α1(III)-CB3, α1(III)-CB7, and α1(III)-CB6, were isolated by carboxymethylcellulose chromatography and Sephadex G-50 SF gel filtration. Automated Edman degradation together with selective hydroxylamine cleavage and chymotrypsin and trypsin digestion enabled determination of their complete amino acid sequence. Compared with type I collagen, the data show tentative homology of α1(III)-CB3 with α1(I)-CBl, α1(I)-CB2, and α1(I)-CB4; al(III)-CB7 with α1(I)-CB5; and α1(III)-CB6 with the amino-terminal portion of α1(I)-CB8. Close interspecies homology was found between the sequences presented here with 90 residues of α1(III)-CB3 and 26 of α1(III)-CB8 of calf aorta. The present study establishes the amino acid sequence of 229 residues near the amino terminus or nearly one-quarter of the type III collagen chains. The disaccharide, Glc-Gal, was convalently bound to hydroxylysine at a position corresponding to the same location in the a 1(1) chain.

UR - http://www.scopus.com/inward/record.url?scp=0017340448&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017340448&partnerID=8YFLogxK

U2 - 10.1021/bi00625a020

DO - 10.1021/bi00625a020

M3 - Article

VL - 16

SP - 1158

EP - 1164

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 6

ER -