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At least 19 recordsLinked 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↗
PubMed1979

Biochemical characterization of guanidinium chloride-soluble dentine collagen from lathyritic-rat incisors.

alpha- and beta-Chains were isolated by sequential ion-exchange and gel-filtration chromatography of guanidinium chloride-soluble dentine collagen obtained from Tris/NaCl-extracted EDTA-demineralized lathyritic-rat incisors. The alpha-chains were identified as alpha 1 I and alpha 2 by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and amino acid analysis of the intact chains and their CNBr peptides. The dentine alpha-chains exhibited higher lysine hydroxylation and phosphate content, but lower hydroxylysine glycosylation, than alpha-chains from skin. Increased lysine hydroxylation was observed in the helical sequences. The alpha 1 I/alpha 2 ratio was approx. 3:1, and was presumably due to the presence of (alpha 1 I)3 molecules along with (alpha 1 I)2 alpha 2 molecules as shown recently for neutral-salt-soluble dentine collagen [Wohllebe & Carmichael (1978) Eur. J. Biochem. 92, 183--188]. In the borohydride-reduced beta 11- and beta 12-chains from guanidinium chloride-soluble dentine collagen, the reduced cross-links hydroxylysinohydroxynorleucine and hydroxylysinonorleucine were present. A higher proportion of hydroxylysinonorleucine in the reduced beta 12-chain probably reflects differences in extent of hydroxylation of specific lysine residues of the alpha 1 I- and alpha 2-chains.

Amino Acids↗
PubMed1990

Estimating age through the amino acid racemization of acid-soluble dentinal peptides.

We studied the possibility of estimating age through the amino acid racemization of acid-soluble dentinal peptide (SP). The correlation of the D/L ratio of aspartic acid and the actual age was the highest in the SP extracted with 1 M HCl (r = 0.996, sigma = +/- 0.8), followed by the total amino acids (TAA:r = 0.995, sigma = +/- 1.0), and the SP extracted with 2 M HCl (r = 0.980, sigma = +/- 1.9) and then SP extracted with 5 M HCl (r = 0.951, sigma = +/- 2.7). The rate of the racemization reaction decreased in the order of SP extracted with 1 M HCl, 2 M HCl, 5 M HCl and the total amino acids (TAA). Consequently, an extraction with 1 M HCl seemed best for estimating the age from SP to serve actual cases.

Age Determination by Teeth↗
PubMed1978

Adhesive bonding of various materials to hard tooth tissues--solubility of dentinal smear layer in dilute acid buffers.

While the acid etch technique has largely solved the problem of bonding restorative materials to enamel, attempts to improve adhesive bonding to dentin have so far had only limited success. One aspect to which insufficient attention has been paid is the presence of a smear layer on cut surfaces and of pellicle on surfaces exposed to saliva, both of which would reduce or prevent durable adhesive bonds. The present study attempts to evaluate the usefulness of various acidic solutions in removing these surface layers while causing minimal damage to the vital contents of the dentinal tubules. A series of twelve 0.16 M buffer solutions were applied to cut dentin surfaces which were then washed, dried and sputter-coated with gold/palladium in preparation for examination by scanning electron microscopy. It is concluded that the smear layer on cut dentin surfaces can be substantially removed in vitro by a 30 second exposure to an isotonic solution of buffered monobasic acids having pKa values between 3.8 and 2.5. Since these solutions did not always remove material from grooves in the prepared surface clinical techniques should aim at producing a smooth cut surface. The response of the vital pulp to this treatment still awaits investigation.

Acid Etching, Dental↗
PubMed1992

Adsorption of dentine proteins onto spheroidal calcium phosphate in a neutral and in an acidic environment.

The adsorption of four different dentine protein fractions onto hydroxyapatite (HAP) was investigated in a nearly neutral (pH 6.7) and in an acidic environment (pH 5.0). The soluble dentine proteins were isolated according to their extractability in successively: 4M guanidine-HCl (GuHCl), 0.5M acetic acid pH 3 (after extraction with GuHCl), and 0.01M EDTA pH 7.4 and 0.1M EDTA pH 7.4 (after complete demineralization with acetic acid). The amounts isolated were 1.2, 3.3, 6.1 and 3.7 mg protein per gram dentine, respectively. The GuHCl extractable proteins exhibited the lowest affinity and the acetic acid extractable proteins the highest affinity for HAP. Acetic acid extractable proteins, were significantly less adsorbed than the other protein fractions at pH 5.0. The maximum adsorbed amount of these proteins increased with decreasing pH which indicated that all the soluble dentine proteins, except perhaps those that one GuHCl-extractable have to be considered as potential demineralization inhibitors.

Acids↗
PubMed1990

Release of organic matrix components from bovine incisor roots during in vitro lesion formation.

The solubilization of organic matrix components during demineralization of powdered and intact root sections from adult bovine incisors was investigated. Root powder was demineralized with 0.1 mol/L acetic acid, pH 4.0, at 4 degrees C and 37 degrees C. Surfaces of intact root sections were subjected to 0.1 mol/L acetic acid, pH 4.0 (for production of erosive lesions), or to 0.1 mol/L lactic acid, 0.2 mmol/L methane hydroxy diphosphonate, pH 5.0 (for production of subsurface lesions at 37 degrees C). The solubilized organic material was analyzed for collagen, total noncollagenous protein (NCP), organic phosphate (Po), and proteoglycans (PGs), which were measured as chondroitin 4-sulfate (C-4-S). For root powder, a maximal release of NCPs and PGs was found only after neutralization of the extraction mixture. For both temperatures tested, the average amounts of liberated noncollagenous components (NCCs) were the same, i.e., 0.68 micrograms [NCP - Po], 0.11 microns Po, and 0.10 micrograms C-4-S per mumols released calcium. The amino acid composition of the NCP fraction revealed relatively high amounts of aspartic acid and serine. These findings indicate that the NCCs were easily liberated from the tissue, and that the NCP fraction consisted mainly of phosphoprotein. Demineralization of intact root sections resulted in average amounts of solubilized NCCs of 0.21 micrograms [NCP - Po], less than 0.01 micrograms Po, and less than 0.01 micrograms C-4-S per mumols released calcium, independent of incubation time and lesion type. The amino acid composition of all NCP fractions was virtually the same, high in glutamic acid, but lower in aspartic acid and serine when compared with the neutralized powder extracts. For both demineralization solutions, the amounts of solubilized collagen were 0.07 and 0.16 micrograms per micromol released calcium after three and 28 days of incubation, respectively. Our experiments indicate that phosphoprotein and proteoglycans may be released from root surfaces during the periods of neutral pH that follow acid demineralization.

Amino Acids↗