Amino Acid Sequence of Cyanogen Bromide Peptides from the Amino-Terminal Region of Chick Skin Collagen

Andrew Kang, Jerome Gross

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

The amino acid sequence of three cyanogen bromide peptides derived from the α1 chain of chick skin collagen, α1-CB0, α1-CB1, and α1-CB2, and of one peptide derived from the α2 chain, α2-CB1, has been determined. α1-CB0, a dipeptide, is the NH2-terminal peptide of α1. α1-CB1 is a septadecapeptide and the next in position. It contains the lysyl residue involved in the formation of the intramolecular cross-link. Next in position is α1-CB2 containing 36 amino acid residues. Thus, the sequence of 55 residues from the NH2 terminus of the α1 chain of chick skin collagen is now established. α2-CB1 is the NH2-terminal peptide of the α2 chain and contains 15 amino acid residues. It also contains the precursor lysyl residue for the intramolecular cross-link. The sequence of the three NH2-terminal peptides of the α1 chain of the chick skin collagen (α1-CB0, α1-CB1, and α1-CB2) is quite homologous to the known sequence of the corresponding region of rat skin collagen. The only differences are substitution of alanine for serine at the positions 14 and 22 and those related to the degree of hydroxylation of certain prolyl residues. However, the sequence of α2-CB1 of chick skin collagen is markedly different from that of α2-CB1 of rat skin collagen. The relatively strict preservation of the sequence of the α1 chain between the collagens from two different classes of vertebrates and the comparatively large differences in the sequence of the α2 chain, at least as far as is presently known, suggest the possibility that the α2 chain may subserve a special function in determining the species-specific properties of collagen. The sequence presented here indicates that the NH2-terminal regions of the α1 and α2 chains could not exist in the helical forms characteristic of the main body of the native collagen molecule. This is consistent with the known susceptibility of this region of the molecule to a variety of proteolytic enzymes and also with its involvement as a cross-linking site.

Original languageEnglish (US)
Pages (from-to)796-804
Number of pages9
JournalBiochemistry
Volume9
Issue number4
DOIs
StatePublished - Feb 1 1970
Externally publishedYes

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Cyanogen Bromide
Amino Acid Sequence
Skin
Collagen
Amino Acids
Peptides
Rats
Hydroxylation
Molecules
Dipeptides
Alanine
Serine
Vertebrates
Peptide Hydrolases
Substitution reactions

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Amino Acid Sequence of Cyanogen Bromide Peptides from the Amino-Terminal Region of Chick Skin Collagen. / Kang, Andrew; Gross, Jerome.

In: Biochemistry, Vol. 9, No. 4, 01.02.1970, p. 796-804.

Research output: Contribution to journalArticle

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abstract = "The amino acid sequence of three cyanogen bromide peptides derived from the α1 chain of chick skin collagen, α1-CB0, α1-CB1, and α1-CB2, and of one peptide derived from the α2 chain, α2-CB1, has been determined. α1-CB0, a dipeptide, is the NH2-terminal peptide of α1. α1-CB1 is a septadecapeptide and the next in position. It contains the lysyl residue involved in the formation of the intramolecular cross-link. Next in position is α1-CB2 containing 36 amino acid residues. Thus, the sequence of 55 residues from the NH2 terminus of the α1 chain of chick skin collagen is now established. α2-CB1 is the NH2-terminal peptide of the α2 chain and contains 15 amino acid residues. It also contains the precursor lysyl residue for the intramolecular cross-link. The sequence of the three NH2-terminal peptides of the α1 chain of the chick skin collagen (α1-CB0, α1-CB1, and α1-CB2) is quite homologous to the known sequence of the corresponding region of rat skin collagen. The only differences are substitution of alanine for serine at the positions 14 and 22 and those related to the degree of hydroxylation of certain prolyl residues. However, the sequence of α2-CB1 of chick skin collagen is markedly different from that of α2-CB1 of rat skin collagen. The relatively strict preservation of the sequence of the α1 chain between the collagens from two different classes of vertebrates and the comparatively large differences in the sequence of the α2 chain, at least as far as is presently known, suggest the possibility that the α2 chain may subserve a special function in determining the species-specific properties of collagen. The sequence presented here indicates that the NH2-terminal regions of the α1 and α2 chains could not exist in the helical forms characteristic of the main body of the native collagen molecule. This is consistent with the known susceptibility of this region of the molecule to a variety of proteolytic enzymes and also with its involvement as a cross-linking site.",
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N2 - The amino acid sequence of three cyanogen bromide peptides derived from the α1 chain of chick skin collagen, α1-CB0, α1-CB1, and α1-CB2, and of one peptide derived from the α2 chain, α2-CB1, has been determined. α1-CB0, a dipeptide, is the NH2-terminal peptide of α1. α1-CB1 is a septadecapeptide and the next in position. It contains the lysyl residue involved in the formation of the intramolecular cross-link. Next in position is α1-CB2 containing 36 amino acid residues. Thus, the sequence of 55 residues from the NH2 terminus of the α1 chain of chick skin collagen is now established. α2-CB1 is the NH2-terminal peptide of the α2 chain and contains 15 amino acid residues. It also contains the precursor lysyl residue for the intramolecular cross-link. The sequence of the three NH2-terminal peptides of the α1 chain of the chick skin collagen (α1-CB0, α1-CB1, and α1-CB2) is quite homologous to the known sequence of the corresponding region of rat skin collagen. The only differences are substitution of alanine for serine at the positions 14 and 22 and those related to the degree of hydroxylation of certain prolyl residues. However, the sequence of α2-CB1 of chick skin collagen is markedly different from that of α2-CB1 of rat skin collagen. The relatively strict preservation of the sequence of the α1 chain between the collagens from two different classes of vertebrates and the comparatively large differences in the sequence of the α2 chain, at least as far as is presently known, suggest the possibility that the α2 chain may subserve a special function in determining the species-specific properties of collagen. The sequence presented here indicates that the NH2-terminal regions of the α1 and α2 chains could not exist in the helical forms characteristic of the main body of the native collagen molecule. This is consistent with the known susceptibility of this region of the molecule to a variety of proteolytic enzymes and also with its involvement as a cross-linking site.

AB - The amino acid sequence of three cyanogen bromide peptides derived from the α1 chain of chick skin collagen, α1-CB0, α1-CB1, and α1-CB2, and of one peptide derived from the α2 chain, α2-CB1, has been determined. α1-CB0, a dipeptide, is the NH2-terminal peptide of α1. α1-CB1 is a septadecapeptide and the next in position. It contains the lysyl residue involved in the formation of the intramolecular cross-link. Next in position is α1-CB2 containing 36 amino acid residues. Thus, the sequence of 55 residues from the NH2 terminus of the α1 chain of chick skin collagen is now established. α2-CB1 is the NH2-terminal peptide of the α2 chain and contains 15 amino acid residues. It also contains the precursor lysyl residue for the intramolecular cross-link. The sequence of the three NH2-terminal peptides of the α1 chain of the chick skin collagen (α1-CB0, α1-CB1, and α1-CB2) is quite homologous to the known sequence of the corresponding region of rat skin collagen. The only differences are substitution of alanine for serine at the positions 14 and 22 and those related to the degree of hydroxylation of certain prolyl residues. However, the sequence of α2-CB1 of chick skin collagen is markedly different from that of α2-CB1 of rat skin collagen. The relatively strict preservation of the sequence of the α1 chain between the collagens from two different classes of vertebrates and the comparatively large differences in the sequence of the α2 chain, at least as far as is presently known, suggest the possibility that the α2 chain may subserve a special function in determining the species-specific properties of collagen. The sequence presented here indicates that the NH2-terminal regions of the α1 and α2 chains could not exist in the helical forms characteristic of the main body of the native collagen molecule. This is consistent with the known susceptibility of this region of the molecule to a variety of proteolytic enzymes and also with its involvement as a cross-linking site.

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