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PMID: 116736 Published · ppublish English Journal Article

EDTA soluble protein of human mature normal enamel.

Calcified tissue international ·Vol. 28 ·No. 3 ·1979-11-06 ·Pages 227-31

Belcourt A, Gillmeth S

Abstract

Pure human mature enamel was prepared using a careful microdissection technique. After EDTA dissolution, the soluble proteins were recovered representing a concentration of 0.035% in the initial enamel. When the samples were analyzed with polyacrylamide gel electrophoresis, Coomassie Brilliant Blue staining revealed only one sharp fast migrating band, whereas o-toluidine blue, methylene blue, Amido Black 10B, and pyronine red G showed a thin double band at the same migration distance. Ultracentrifugation studies suggested that the proteins were of low molecular weight or of weak density. Absorption spectra showed a strong absorbance at 260 nm. After hydrolysis, amino acid analyses yielded a composition of 25% Gly, 13.5% Glu, 11% Ser, and 11% Pro. Cysteine measured as cysteic acid was present at 2%, and 2% hydroxyproline was found. A carbohydrate content of 15% was estimated by the anthrone method. Glucose, galactose, mannose, and fucose, identified through gas chromatography, were in a molar ratio of 9:4:3:1. Thus the organic matrix of adult human enamel consists of one or possibly two acidic glycoproteins.

MeSH Terms
Amino Acids/analysis Carbohydrates/analysis Dental Enamel Proteins/analysis Edetic Acid Electrophoresis, Polyacrylamide Gel Glycoproteins/analysis Humans Molecular Weight Solubility
Chemicals
Amino Acids Carbohydrates Dental Enamel Proteins Glycoproteins Edetic Acid
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Belcourt A
Gillmeth S
References (19)
19 references, click to expand
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Article Info
Journal
Calcified tissue international
Abbr.
Calcif Tissue Int
ISSN
0171-967X
Published
1979-11-06
Pages
227-31
Language
English
Region
United States
NLM ID
7905481
Subset
IM
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