MOLECULAR INTERFACE CHARACTERIZATION IN HUMAN BONE-MATRIX .1. BIOCHEMICAL AND IR SPECTROSCOPIC STUDIES

被引：18

作者：

RAIF, EM ^{[1
]}

HARMAND, MF ^{[1
]}

机构：

[1] UNIV BORDEAUX 2, INSERM, U306, F-33076 BORDEAUX, FRANCE

来源：

BIOMATERIALS | 1993年 / 14卷 / 13期

关键词：

BONE; MINERAL CONTENT; COLLAGEN;

D O I：

10.1016/0142-9612(93)90189-9

中图分类号：

R318 [生物医学工程];

学科分类号：

0831 ;

摘要：

The aim of this work is the characterization of interfaces in calcified tissues. In order to separate the non-collagenous bone proteins, according to their interaction with collagen or hydroxyapatite crystals 10 sequential bone demineralizations using EDTA alone were carried out, followed by four sequential extractions using both EDTA and GuHCl. The extracts were characterized by SDS-PAGE, IR spectrum analysis, and kinetics of demineralization and proteins released. A great proportion of non-collagenous proteins are bound to the collagen matrix, many of which have a high affinity to it. This work demonstrates that collagen is not directly linked to the mineralized phase.

引用

页码：978 / 984

页数：7