Chromatographic studies of carbohydrate components in enamel

Burgess, R.C.; Nikiforuk, Gordon; Maclaren, Catherine

doi:10.1016/0003-9969(60)90013-3

Cited by 12 publications

(2 citation statements)

References 28 publications

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“…Similar studies involving more drastic alterations of dietary carbohydrate levels would be most interesting. Chemical analyses have confirmed the persistence of carbohydrates in mature enamel (Burgess, Nikiforuk & Maclaren, 1960), and some have suggested that these are influenced by the carbohydrate content of the diet during tooth development (Egyedi, 1953U,b;Buxbaum, Kohn, Proutt & Oster, 1957;O'Day & Bavetta, 1962).…”

Section: Carbohydrates and Nutrition '33mentioning

confidence: 99%

The systemic influence of carbohydrates on teeth

Speirs

1964

Proc. Nutr. Soc.

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Section: Carbohydrates and Nutrition '33mentioning

confidence: 99%

The systemic influence of carbohydrates on teeth

Speirs

1964

Proc. Nutr. Soc.

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“…and 42%, respectively [2-4]. Citrate and lactate ions are also present in microquantities [5], whereas only traces of carbohydrate have been detected [6].Many studies have reported amino acid compositions for the human enamel matrix [7][8][9][10][11][12][13][14]. The main amino acids described were alanine, glutamic acid, glycine, proline, and serine.…”

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confidence: 98%

EDTA soluble protein of human mature normal enamel

Belcourt

Gillmeth

1979

Calcif Tissue Int

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Pure human mature enamel was prepared using a careful microdissection technique. After EDTA dissolution, the soluble proteins were recovered representing a concentration of 0.035% in the initial enamel. When the samples were analyzed with polyacrylamide gel electrophoresis, Coomassie Brilliant Blue staining revealed only one sharp fast migrating band, whereas o-toluidine blue, methylene blue, Amido Black 10B, and pyronine red G showed a thin double band at the same migration distance. Ultracentrifugation studies suggested that the proteins were of low molecular weight or of weak density. Absorption spectra showed a strong absorbance at 260 nm. After hydrolysis, amino acid analyses yielded a composition of 25% Gly, 13.5% Glu, 11% Ser, and 11% Pro. Cysteine measured as cysteic acid was present at 2%, and 2% hydroxyproline was found. A carbohydrate content of 15% was estimated by the anthrone method. Glucose, galactose, mannose, and fucose, identified through gas chromatography, were in a molar ratio of 9:4:3:1. Thus the organic matrix of adult human enamel consists of one or possibly two acidic glycoproteins.

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The biosynthesis and secretion of precursor enamel protein by ameloblasts as visualized by autoradiography after tryptophan administration

1976

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The incorporation of 3H-tryptophan into the inner enamel epithelium of newborn mouse incisor tooth organs has been studied in situ by light and electron microscopic autoradiography to determine the sites and kinetics of biosynthesis, migration, and secretion of precursor enamel protein during newborn mouse incisor tooth formation maxillary and mandibular incisor tooth amelogenesis was studied 5, 30, 60, 120, 240 minutes and 24 hours following the intraperitoneal injection of 3H-tryptophan. By 5 minutes, 40% of the total silver grains associated with the secretory ameloblasts were localized over the rough endoplasmic reticulum and 50% of the silver grains were localized over the Golgi apparatus. By 30 minutes, silver grains were observed predominately over condensing vacuoles and secretory granules within the forming Tomes' processes, and were also localized over the extracellular "granular" pre-enamel matrix. The enamel proteins were synthesized on membrane-bound polysomes, transferred within the cisternae of the rough endoplasmic reticulum and then accumulated in the inner saccules of the Golgi apparatus. The enamel proteins were than packaged in condensing vacuoles which subsequently became secretory granules which migrated to the lateral and apical secretory regions of the forming Tomes' processes. It was concluded from these in vivo studies that enamel protein were synthesized and subsequently secreted within 30 minutes. The initially secreted precursor enamel protein was localized over a material which demonstrated a granular or stippled ultrastructure. The labeled protein then was localized over the amorphous enamel matrix per se which contained the forming calcium hydroxyapatite crystals. We assumed, therefore, that there are two different ultrastructural forms of 3H-tryptophan containing extracellular enamel proteins and suggest that the granular or "stippled" form represents newly secreted precursor enamel protein.

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Chromatographic studies of carbohydrate components in enamel

Cited by 12 publications

References 28 publications

The systemic influence of carbohydrates on teeth

The systemic influence of carbohydrates on teeth

EDTA soluble protein of human mature normal enamel

The biosynthesis and secretion of precursor enamel protein by ameloblasts as visualized by autoradiography after tryptophan administration

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