SEQUENCE-ANALYSIS OF A FULL-LENGTH CDNA FOR THE MURINE PRO-ALPHA-2(I) COLLAGEN CHAIN - COMPARISON OF THE DERIVED PRIMARY STRUCTURE WITH HUMAN PRO-ALPHA-2(I) COLLAGEN

被引：23

作者：

PHILLIPS, CL ^{[1
]}

MORGAN, AL ^{[1
]}

LEVER, LW ^{[1
]}

WENSTRUP, RJ ^{[1
]}

机构：

[1] DUKE UNIV,MED CTR,DEPT PEDIAT,DIV GENET & METAB,DURHAM,NC 27710

来源：

GENOMICS | 1992年 / 13卷 / 04期

关键词：

D O I：

10.1016/0888-7543(92)90065-Z

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Comparison of the nucleotide sequence and primary structure of murine and human proα2(I) collage indicates a high degree of homology: 87% at the nucleotide level and 87% at the amino acid level, with the greatest degree of variability in the amino- and carboxy-propeptide domains. The homology is greatest in the triple helical domain, repeating [Gly-X-Y]338, exhibiting 90% homology at the amino acid level, with only X and Y position residue substitutions. The X and Y residues show 86% homology between murine and human proα2(I) collagen triple helices, with no truly nonconservative substitutions. © 1992.

引用

页码：1345 / 1346

页数：2

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