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Acta Odontologica Scandinavica Volume 44, 1986 - Issue 2
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Original Article

Effects of different extraction media on the electrophoretic pattern of proteins from partly mineralized bovine enamel

Elisabeth Sailing General Clinic, Institute of Biochemistry and Oral Anatomy, The Royal Dental College, The Panum Institute, Copenhagen, Denmark
,
Dennis Moe General Clinic, Institute of Biochemistry and Oral Anatomy, The Royal Dental College, The Panum Institute, Copenhagen, Denmark
&
Svend Kirkeby General Clinic, Institute of Biochemistry and Oral Anatomy, The Royal Dental College, The Panum Institute, Copenhagen, Denmark
Pages 91-94 | Received 07 Nov 1984, Published online: 02 Jul 2009
 
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Abstract

Five different extraction solutions were used to isolate matrix proteins from immature bovine enamel, to evaluate the effect of this procedure on the pattern obtained after electrophoresis. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the dominating protein fraction in the ethylenediaminetetraacetic acid extract had a molecular weight of 67,000 daltons. The acetic acid and phosphate buffer extracts contained mostly low molecular weight proteins. Isoelectric focusing showed that most of the enamel proteins had isoelectric poinits below pH7.0.

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