Complete amino acid sequence of amelogenin in developing bovine enamel

Relative molecular mass determination of a major, highest relative molecular mass extracellular amelogenin of developing bovine enamel

“…The -40% lower value for the M,, calculated using CNBr peptides of collagen as standards, is very close to the values obtained for 4 of the major homogeneous fractions of developing bovine enamel (16 1 OO-16 800) by sedimentationequilibrium ultracentrifugation reported earlier [5], and to the value obtained in the present study by sedimentation-equilibrium ultracentrifugation. These experimental data, together with the value for the M, calculated from recent amino acid sequence studies (-19000) [17], lead us to conclude that the true Mr of this major, high il& amelogenin, falls in the range of 15000-19000. Thus, as far as the major question posed, namely, what is the relationship between the previously described 15 000-17 000-Da amelogenin components and the more recently isolated component of allegedly 26000-30000-Da which was presumed to be a new high iK amelogenin, we conclude that they are the same component(s), the recently reported it4, of 26000-30000 [7,8] being in error.…”

“…The partial specific volume, V, of bovine amelogenin [17] was calculated using the method of Cohn and Edsall [18]:…”

“…In the calculation, the values of Ni from [17] were used. The values for Vi of the amino acid residues were adapted from [19] except for Vi 0.50 of Ser(P) [20].…”

The Enamel Protein Amelogenin Binds to the N-Acetyl-d-glucosamine-mimicking Peptide Motif of Cytokeratins

“…They consist of a single polypeptide chain of some 180 amino acids and are highly conserved across species. Further, there is some variation in amelogenin protein size between species and also as a result of alternative splicing of the primary RNA (15,(23)(24)(25)(26). Concomitant with enamel biomineralization, the primary amelogenin is proteolytically processed from the C-terminal end to smaller fragments, among which TRAP, consisting of the 45 N-terminal residues, is prominent (27-29).…”

A histochemical study on lectin binding in the immature enamel and secretory ameloblasts of rat incisors.

“…Enamel proteins, 90 to 100% of the organic matrices, are glycoproteins designated as amelogenin and enamelin (Termine et al 1980 ;Robinson and Kirkham 1986). Their amino acid compositions are studied very well in several species (Eastoe 1979 ;Termine et al 1980 ;Fincham et al 1982 ;Slavkin et al 1982), and partial and complete amino acid sequences of amelogenin are reported in some species (Fincham et al 1981(Fincham et al , 1983Takagi et al 1984 ;Snead et al 1985). The similarity in composition and sequence of their amino acids among species suggests that they have same biological activities in many species.…”