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

Authors

  • 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

DOI:

https://doi.org/10.3109/00016358609041313

Keywords:

Composition, isoelectric focusing, SDS-PAGE

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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Published

1986-01-01

Issue

Vol. 44 No. 2 (1986): Acta Odontologica Scandinavica

Section

Articles