PubMed Health⌕ Search

Biomedical subjects

A G Fincham

Publications and source records attributed to A G Fincham.

At least 73 records · Page 4Linked to original sources
PubMed1982

Neonatal hamster molar tooth development: extraction and characterization of amelogenins, enamelins, and soluble dentin proteins.

Amelogenins, enamelins, and soluble dentin proteins were sequentially separated under dissociative conditions from morphologically characterized molar tooth germs of 4-, 6-, and 7-day-old hamsters. Polyacrylamide gel electrophoretic, gel filtration chromatographic, and amino acid compositional data of neonatal hamster amelogenin extracts were in general agreement with those obtained from fetal bovine enamel under similar extraction conditions. As development progressed (e.g., 4 vs. 7 days of life), changes in amelogenin proteins were manifested by altered values of all biochemical parameters measured. A high molecular weight (approximately 160,000-200,000 daltons) Stains-All-positive protein band was observed for all hamster enamelin extracts on SDS gels. Amino acid compositional data from this "enamel crystal protein," partially purified by dissociative gel-filtration chromatography, are presented. The hamster dentin phosphoprotein was partially purified by ion-exchange chromatography in 7M urea. The molecular weight (75,000-80,000 daltons) and amino acid composition of this protein were similar to those of rat incisor dentin phosphoprotein, but different from those of the fetal bovine phosphoprotein.

Amelogenin↗
PubMed1982

Comparative protein biochemistry of developing dental enamel matrix from five mammalian species.

The matrix proteins of the developing dental enamel of five mammalian species were isolated and subjected to chromatographic, electrophoretic, and amino acid analyses. It was found that the principal chromatographic fractions showed similarities of both size and amino acid composition among species. The major amelogenin protein of the cow, hamster, human, and sheep was of about 30,000 daltons and of the pig enamel matrix about 20,000 daltons. In each species a higher molecular weight fraction, greater than 40,000 daltons, was detected. In the lower molecular weight range an amelogenin polypeptide enriched in leucine, a fraction rich in tyrosine, and a fraction of intermediate size (Bovine matrix "Component-14") were identified in each case. It is suggested that these characteristic proteins arise during the degradation of the matrix which accompanied mineralization.

Amelogenesis↗
PubMed1981

Dental enamel matrix: sequences of two amelogenin polypeptides.

The amino acid sequences of a leucine-rich amelogenin polypeptide (LRAP) and a tyrosine-rich amelogenin polypeptide (TRAP), isolated from foetal bovine enamel matrix, were determined. Both LRAP and TRAP occurred in two forms; in each case, one of the molecular species appeared to be shortened at the COOH terminus by 2 and 4 residues, respectively. A striking finding was that LRAP and TRAP had identical sequences for the first 33 residues but were almost completely different for the remaining 12 amino acids.

Amelogenin↗
PubMed1979

A simple procedure for the isolation of a major amelogenin polypeptide component.

A simple, reproducible gel-filtration procedure for the isolation of one of the major 'J-Group' polypeptides of the bovine foetal dental-enamel matrix is described. The purified polypeptide was characterized by amino acid analysis, electrophoresis, cleavage with CNBr and N-terminal analyses. The isolated component is shown to be closely similar to an amelogenin component described by other workers.

Amino Acids↗
PubMed1979

The amelogenin problem: a comparison of purified enamel matrix proteins.

Using a combination of gel filtration and DEAE-cellulose chromatography, together with small-scale preparative polyacrylamide gel electrophoresis, we isolated five proteins (amelogenins) from demineralized bovine fetal dental enamel matrix. These purified proteins were characterized by amino acid analysis and gel electrophoresis. Comparisons of these data with those of other workers suggest that, although there are similarities in the published data between components of comparable electrophoretic mobility, there are gross differences in the reported amino acid compositions. It is suggested that these differences are due not to separative problems arising from reversible aggregations, but to inadequate comparisons of the electrophoretic and amino acid analytical data.

Amelogenesis↗
PubMed1979

Dental enamel matrix--isolation and partial sequence of a peptide component.

Chromatography of demineralized bovine fetal enamel matrix proteins on 'Biogel P6' was shown to yield a trailing peak which contained a single electrophoretic component. This polypeptide, further purified by chromatography on 'Biogel P4', was found to be homogeneous by disc electrophoresis and gel isoelectric focussing. Amino acid analyses indicated this component (designated: "E5') to be similar to some of the phosphopeptides previously described. Cyanogen bromide cleavage of E5 yielded three principal products whose amino acid compositions and N-terminal residues were investigated. A partial sequence for component E5 was proposed and comparison with previous bovine matrix isolates was made.

Amino Acid Sequence↗
PubMedDate not supplied

Self-assembly of a recombinant amelogenin protein generates supramolecular structures.

Amelogenin proteins are the principal constituents of the extracellular organic matrix associated with the nucleation and growth of the carbonated calcium hydroxyapatite (HAP)-containing mineral phase of dental enamel. Amelogenins are believed to function in controlling the sizes and organization of the developing enamel crystals. Previous studies have shown that enamel proteins exhibit unusual reversible aggregation properties. The present studies were designed to test the hypothesis that self-assembly of recombinant amelogenin generates supramolecular structures that are indistinguishable from the electron-dense particles associated with HAP crystal growth in vivo. A recombinant amelogenin analog of the murine 180-residue protein was analyzed by high-resolution size exclusion chromatography, atomic force (AFM), and transmission electron (TEM) microscopy. It was found that the amelogenin formed supramolecular aggregates which were in a concentration-dependent equilibrium with protein monomers. Imaging of the amelogenin by both AFM and TEM techniques revealed spherical aggregate structures of about 18 nm diameter which were seen to be similar to electron-dense enamel structures observed in vivo. We interpret these results to suggest that, in vivo, the amelogenin protein self-assembles through functional motifs of the protein primary structure, generating specific supramolecular aggregates which we hypothesize function to control the ultrastructural organization of the developing enamel crystallites.

Amelogenin↗