The carbohydrate moiety of mineral-bound proteins from fetal enamel: a basis for enamelins heterogeneity.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis*; D002417:Cattle; D003208:Concanavalin A; D003743:Dental Enamel / Q000032:analysis / Q000196:embryology*; D003746:Dental Enamel Proteins / Q000032:analysis*; D005333:Fetus; D008970:Molecular Weight; D010758:Phosphorus / Q000032:analysis
D000596:Amino Acids; D002241:Carbohydrates; D003746:Dental Enamel Proteins; C038456:tuftelin; D003208:Concanavalin A; D010758:Phosphorus