The amelogenin problem: a comparison of purified enamel matrix proteins.

Abstract:

:Using a combination of gel filtration and DEAE-cellulose chromatography, together with small-scale preparative polyacrylamide gel electrophoresis, we isolated five proteins (amelogenins) from demineralized bovine fetal dental enamel matrix. These purified proteins were characterized by amino acid analysis and gel electrophoresis. Comparisons of these data with those of other workers suggest that, although there are similarities in the published data between components of comparable electrophoretic mobility, there are gross differences in the reported amino acid compositions. It is suggested that these differences are due not to separative problems arising from reversible aggregations, but to inadequate comparisons of the electrophoretic and amino acid analytical data.

journal_name

Calcif Tissue Int

authors

Fincham AG

doi

10.1007/BF02441163

subject

Has Abstract

pub_date

1979-03-13 00:00:00

pages

65-73

issue

1

eissn

0171-967X

issn

1432-0827

journal_volume

27

pub_type

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