ISOLATION AND STRUCTURE OF AMINO-TERMINAL CROSS-LINKING REGION IN INSOLUBLE TYPE-3 COLLAGEN

被引：13

作者：

BECKER, U ^{[1
]}

FIETZEK, PP ^{[1
]}

NOWACK, H ^{[1
]}

TIMPL, R ^{[1
]}

机构：

[1] MAX PLANCK INST BIOCHEM, BINDEGEWEBS FORSCH ABT, D-8033 MARTINSRIED, FED REP GER

来源：

HOPPE-SEYLERS ZEITSCHRIFT FUR PHYSIOLOGISCHE CHEMIE | 1976年 / 357卷 / 10期

关键词：

D O I：

10.1515/bchm2.1976.357.2.1409

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A collagenous peptide T1X was isolated from a tryptic digest of the insoluble matrix of calf skin. The peptide consists of 2 identical polypeptide chains each with a length of 72 amino acid residues joined by a cross-link. Absorption spectra obtained from hydrazone and azine derivatives of T1X indicated that the peptide contains an aldol-type of cross-link (X). The sequence of 23 amino acid residues in the amino-terminal region was determined as Glx-Tyr-Glu-Ala-Tyr-Asp-Val-X-Ser-Gly-Val-Ala-Gly-Gly-Gly-Ile-Ala-Gly-Tyr-Hyp-Gly-Pro-Ala. This sequence overlaps the previously described amino-terminal sequence of .alpha.1 (III) chain obtained from pepsin treated, insoluble type III collagen. The present data demonstrate a nonhelical segment of 14 amino acid residues in type III collagen important for cross-linking.

引用

页码：1409 / 1415

页数：7

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