PROTEINS OF PERIODONTIUM - CHARACTERIZATION OF INSOLUBLE COLLAGENS OF BOVINE DENTAL CEMENTUM
PROTEINS OF PERIODONTIUM - CHARACTERIZATION OF INSOLUBLE COLLAGENS OF BOVINE DENTAL CEMENTUM
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DOI：
10.1007/bf02012764
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发表时间：
1977-01-01
期刊：
影响因子：
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通讯作者：
TAYLOR, RE
中科院分区：
文献类型：
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作者：
BIRKEDALHANSEN, H;BUTLER, WT;TAYLOR, RE
以牛牙骨质不溶性胶原为原料制备溴化氰（CNBr）肽。色谱分离后，通过氨基酸组成鉴定肽。 I 型胶原蛋白 ([α1(I)]2.α2) 占有机基质的 90% 以上，而 III 型胶原蛋白 ([α1(III)]3) 的含量约为 5%。氨基酸分析表明，来自牙骨质的α1(I)和α2链的CNBr肽与来自小牛皮肤的相应肽非常相似。唯一的系统差异是牙骨质肽的脯氨酰和赖氨酰残基的羟基化水平较高。
Cyanogen bromide (CNBr) peptides were prepared of the insoluble collagen of bovine dental cementum. Following chromatographic separation, the peptides were identified by their amino-acid composition. Type I collagen ([.alpha.1(I)]2.alpha.2) accounted for more than 90% of the organic matrix, while Type III collagen ([.alpha.1(III)]3) was present at a level of approximately 5%. Amino-acid analyses revealed that the CNBr peptides from .alpha.1(I) and .alpha.2 chains of cementum closely resembled the corresponding peptides from calf skin. The only systematic difference was a higher level of hydroxylation of prolyl and lysyl residues of the cementum peptides.