Phosphoprotein from dentin. New approaches to achieve and assess purity.

Abstract

Phosphorprotein extracted from rat incisors was purified by passage through a sulfonated polystyrene column. The phosphoprotein that emerged in the void volume contained 54% phosphoserine + serine and 36% aspartic acid and, in contrast to that obtained by DEAE-cellulose chromatography, was devoid of proline, valine, isoleucine, leucine, tyrosine, phenylalanine and arginine. Gel electrophoresis of the material purified on sulfonated polystyrene columns gave one major phosphate-containing band which would not stain with Coomassie Blue. EDTA or acetic acid demineralization yielded phosphoprotein preparations with identical compositions and electrophoretic properties. These data show that purification procedures reported earlier are insufficient.

Statistics

05001000'86'89'92'95'98'01'04'07'10'13'16
Citations per Year

450 Citations

Semantic Scholar estimates that this publication has 450 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Munksgaard1977PhosphoproteinFD, title={Phosphoprotein from dentin. New approaches to achieve and assess purity.}, author={Erik Christian Munksgaard and William T. Butler and William S. Richardson}, journal={Preparative biochemistry}, year={1977}, volume={7 5}, pages={321-31} }