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PMID: 3130169 Published · ppublish English Journal Article

The carbohydrate moiety of mineral-bound proteins from fetal enamel: a basis for enamelins heterogeneity.

Calcified tissue international ·Vol. 42 ·No. 3 ·1988-03-00 ·Pages 196-200

Menanteau J, Meflah K, Strecker G

Abstract

Enamelins were prepared from the soft enamel of bovine fetuses. They were purified on synthetic hydroxyapatite and separated in two fractions by affinity chromatography on a ConA-ultrogel column. The two fractions were different with respect to their electrophoretic behavior, stainability, amino acid composition, phosphorylation, and glycosylation. The ConA-binding fraction, consisting of three molecular species with apparent molecular weights of 33, 37, and 45 kD, contained organic phosphorus and high levels of sugars. The Gal/Man ratio suggested a biantennary structure. The ConA-unbound fraction contained two major molecular species with molecular weights of 70 and 56 kD, and represented 70% of the total enamelin preparation. The amino acid composition of this fraction showed a higher level of alanine and a lower level of proline when compared with that of total enamelins. Its sugar composition was unusual, being principally constituted of N-acetyl galactosamine and N-acetyl glucosamine.

MeSH Terms
Amino Acids/analysis Animals Carbohydrates/analysis Cattle Concanavalin A Dental Enamel/analysis,embryology Dental Enamel Proteins/analysis Fetus Molecular Weight Phosphorus/analysis
Chemicals
Amino Acids Carbohydrates Dental Enamel Proteins tuftelin Concanavalin A Phosphorus
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Menanteau J
INSERM U. 225, UER d'Odontologie, Nantes, France.
Meflah K
Strecker G
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Article Info
Journal
Calcified tissue international
Abbr.
Calcif Tissue Int
ISSN
0171-967X
Published
1988-03-00
Pages
196-200
Language
English
Region
United States
NLM ID
7905481
Subset
IM
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