Literature DB >> 270485

A chromatographic study of the relative affinities of rat bone and skin collagen alpha1 chains for hydroxyapatite.

C F Nawrot, D J Campbell.   

Abstract

The affinity of a bone collagen alpha1 chain for hydroxyapatite has been compared to a similarly isolated skin component from the same animals. The chain from bone exhibits a higher affinity for the mineral. This enhanced affinity appears to be related to its primary structure, specifically its hydroxylysine moieties.

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Year:  1977        PMID: 270485     DOI: 10.1177/00220345770560080401

Source DB:  PubMed          Journal:  J Dent Res        ISSN: 0022-0345            Impact factor:   6.116


  2 in total

1.  Organic-inorganic interaction and the growth mechanism of hydroxyapatite crystals in gelatin matrices between 37 and 80 degrees C.

Authors:  Myung Chul Chang; William H Douglas; Junzo Tanaka
Journal:  J Mater Sci Mater Med       Date:  2006-04       Impact factor: 3.896

2.  Biochemical characterization of guanidinium chloride-soluble dentine collagen from lathyritic-rat incisors.

Authors:  M Wohllebe; D J Carmichael
Journal:  Biochem J       Date:  1979-09-01       Impact factor: 3.857

  2 in total

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