Covalent structure of collagen

Amino acid sequence of an arthritogenic cyanogen bromide peptide from type II collagen of bovine cartilage

Jerome M. SEYER, Karen Hasty, Andrew Kang

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25 Citations (Scopus)

Abstract

Bovine articular type II collagen was prepared by limited pepsin digestion, differential salt fractionation and carboxymethylcellulose chromatography. Cyanogen bromide digestion of purified type II collagen α chains yielded twelve distinct peptides designated CB1–12. The peptide α1(II)‐CB11 was isolated by carboxymethylcellulose chromatography and Sephadex G‐75S gel filtration. Automated Edman degradation together with chymotrypsin, thermolysin and trypsin digestion enabled identification of its complete amino acid sequence. Compared with type I and type III collagen, the data show similarity with α1(I)‐CB8 and α1(III)‐CB6‐1‐8‐10‐2 peptides, respectively. The peptide is located within residues 124–402 of the α1(II) collagen chain and with its identification, now extends the known amino acid sequence of bovine type II cartilage collagen to 660 amino acid residues including α1(II)‐CB1‐2‐6‐12‐11‐8‐10 (partial). This corresponds to α1(I)‐CB0‐1‐2‐4‐5‐8‐3‐7 (partial; 1–660) and α1(III)‐CB3A‐3B‐3C‐7‐6‐1‐8‐10‐2‐4‐5 (partial; 1–660) of bovine α1(I) and α1(III) collagen chains.

Original languageEnglish (US)
Pages (from-to)159-173
Number of pages15
JournalEuropean Journal of Biochemistry
Volume181
Issue number1
DOIs
StatePublished - Jan 1 1989

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Cyanogen Bromide
Cartilage
Collagen Type I
Amino Acid Sequence
Collagen
Amino Acids
Digestion
Peptides
Carboxymethylcellulose Sodium
Chromatography
Thermolysin
Collagen Type III
Pepsin A
Gel Chromatography
Chymotrypsin
Fractionation
Salts
Joints
Trypsin
Degradation

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

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title = "Covalent structure of collagen: Amino acid sequence of an arthritogenic cyanogen bromide peptide from type II collagen of bovine cartilage",
abstract = "Bovine articular type II collagen was prepared by limited pepsin digestion, differential salt fractionation and carboxymethylcellulose chromatography. Cyanogen bromide digestion of purified type II collagen α chains yielded twelve distinct peptides designated CB1–12. The peptide α1(II)‐CB11 was isolated by carboxymethylcellulose chromatography and Sephadex G‐75S gel filtration. Automated Edman degradation together with chymotrypsin, thermolysin and trypsin digestion enabled identification of its complete amino acid sequence. Compared with type I and type III collagen, the data show similarity with α1(I)‐CB8 and α1(III)‐CB6‐1‐8‐10‐2 peptides, respectively. The peptide is located within residues 124–402 of the α1(II) collagen chain and with its identification, now extends the known amino acid sequence of bovine type II cartilage collagen to 660 amino acid residues including α1(II)‐CB1‐2‐6‐12‐11‐8‐10 (partial). This corresponds to α1(I)‐CB0‐1‐2‐4‐5‐8‐3‐7 (partial; 1–660) and α1(III)‐CB3A‐3B‐3C‐7‐6‐1‐8‐10‐2‐4‐5 (partial; 1–660) of bovine α1(I) and α1(III) collagen chains.",
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N2 - Bovine articular type II collagen was prepared by limited pepsin digestion, differential salt fractionation and carboxymethylcellulose chromatography. Cyanogen bromide digestion of purified type II collagen α chains yielded twelve distinct peptides designated CB1–12. The peptide α1(II)‐CB11 was isolated by carboxymethylcellulose chromatography and Sephadex G‐75S gel filtration. Automated Edman degradation together with chymotrypsin, thermolysin and trypsin digestion enabled identification of its complete amino acid sequence. Compared with type I and type III collagen, the data show similarity with α1(I)‐CB8 and α1(III)‐CB6‐1‐8‐10‐2 peptides, respectively. The peptide is located within residues 124–402 of the α1(II) collagen chain and with its identification, now extends the known amino acid sequence of bovine type II cartilage collagen to 660 amino acid residues including α1(II)‐CB1‐2‐6‐12‐11‐8‐10 (partial). This corresponds to α1(I)‐CB0‐1‐2‐4‐5‐8‐3‐7 (partial; 1–660) and α1(III)‐CB3A‐3B‐3C‐7‐6‐1‐8‐10‐2‐4‐5 (partial; 1–660) of bovine α1(I) and α1(III) collagen chains.

AB - Bovine articular type II collagen was prepared by limited pepsin digestion, differential salt fractionation and carboxymethylcellulose chromatography. Cyanogen bromide digestion of purified type II collagen α chains yielded twelve distinct peptides designated CB1–12. The peptide α1(II)‐CB11 was isolated by carboxymethylcellulose chromatography and Sephadex G‐75S gel filtration. Automated Edman degradation together with chymotrypsin, thermolysin and trypsin digestion enabled identification of its complete amino acid sequence. Compared with type I and type III collagen, the data show similarity with α1(I)‐CB8 and α1(III)‐CB6‐1‐8‐10‐2 peptides, respectively. The peptide is located within residues 124–402 of the α1(II) collagen chain and with its identification, now extends the known amino acid sequence of bovine type II cartilage collagen to 660 amino acid residues including α1(II)‐CB1‐2‐6‐12‐11‐8‐10 (partial). This corresponds to α1(I)‐CB0‐1‐2‐4‐5‐8‐3‐7 (partial; 1–660) and α1(III)‐CB3A‐3B‐3C‐7‐6‐1‐8‐10‐2‐4‐5 (partial; 1–660) of bovine α1(I) and α1(III) collagen chains.

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