Seyer J M, Hasty K A, Kang A H
Connective Tissue Research Laboratory, Veterans Administration Medical Center, Memphis, TN 38104.
Eur J Biochem. 1989 Apr 15;181(1):159-73. doi: 10.1111/j.1432-1033.1989.tb14707.x.
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 alpha chains yielded twelve distinct peptides designated CB1-12. The peptide alpha 1(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 alpha 1(I)-CB8 and alpha 1(III)-CB6-1-8-10-2 peptides, respectively. The peptide is located within residues 124-402 of the alpha 1(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 alpha 1(II)-CB1-2-6-12-11-8-10 (partial). This corresponds to alpha 1(I)-CB0-1-2-4-5-8-3-7 (partial; 1-660) and alpha 1(III)-CB3A-3B-3C-7-6-1-8-10-2-4-5 (partial; 1-660) of bovine alpha 1(I) and alpha 1(III) collagen chains.
牛关节II型胶原蛋白通过有限的胃蛋白酶消化、分级盐析和羧甲基纤维素色谱法制备。对纯化的II型胶原蛋白α链进行溴化氰消化，产生了12种不同的肽，命名为CB1 - 12。肽α1(II)-CB11通过羧甲基纤维素色谱法和Sephadex G - 75S凝胶过滤分离出来。自动Edman降解结合胰凝乳蛋白酶、嗜热菌蛋白酶和胰蛋白酶消化能够鉴定其完整的氨基酸序列。与I型和III型胶原蛋白相比，数据分别显示与α1(I)-CB8和α1(III)-CB6 - 1 - 8 - 10 - 2肽相似。该肽位于α1(II)胶原蛋白链的124 - 402位残基内，随着其鉴定，现在将牛II型软骨胶原蛋白的已知氨基酸序列扩展到660个氨基酸残基，包括α1(II)-CB1 - 2 - 6 - 12 - 11 - 8 - 10（部分）。这对应于牛α1(I)和α1(III)胶原蛋白链的α1(I)-CB0 - 1 - 2 - 4 - 5 - 8 - 3 - 7（部分；1 - 660）和α1(III)-CB3A - 3B - 3C - 7 - 6 - 1 - 8 - 10 - 2 - 4 - 5（部分；1 - 660）。
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