Bovine dentin

Boonstra WD, De Vries J, Ten Bosch JJ, Ogaard B and Arends J (1993) Inhibition of bovine dentin demineralization by a glutardialdehyde pretreatment an in vitro caries study. Scand J Dent Res 101, 72-77. 

Kuboki Y, Tsuzaki M, Sasaki S, Liu CF and Mechanic GL (1981) Location of the intermolecular cross-links in bovine dentine collagen, solubilization with trypsin and isolation of cross-link peptides containing dihydroxylysinonorleucine and pyridinoline. Biochem Biophys Res Comm 102, 119-126. 

The aim of this study was to find proof that the Maillard reaction can take place in demineralized dentin. Markers for the initial and advanced Maillard reaction as well as physiological cross-links were investigated after incubation of bovine dentin with glucose. Changes in susceptibility to protein-degrading enzymes and in fluorescence specific for the reaction were additionally measured. 

Collagen determination. In order to calculate the amount of collagen in a sample, hydroxyproline was measured in acid hydrolyzates (Jamall et al., 1981). After oxidation, hydroxyproline reacts with p-dimethyl-aminobenzaldehyde to give a red colour, which is measured by spectrophotometry. For bovine dentin, collagen mass was estimated as 8.0 x the hydroxyproline value as calculated from previous data (Volpin and Veis, 1973). To calculate the molar quantities of collagen, a molecular mass of 300 kDa was used. 

V, and Vlll unknown amino acids from bovine dentin. 

A NOVEL PYRROLENINONE CROSS-LINK FROM BOVINE DENTIN ... 

A novel pyrroleninone cross-link from bovine dentin... 

Separation of a purified hydrolyzate of demineralized bovine dentin by cation exchange chromatography at pH 5.25. Gradient 0.0 - 0.5 M NaCl in 0.05 M HAc/NaAc, 1 mM NaNs, pH 5.25. Column SP Sephadex C25 (34 x2.6cm). Flow rate approx. 30 ml/h. The 4-ml fractions were assayed for amino acids by ninhydrin reaction (—) and for NaCl by electric conductivity measurement after 75-fold dilution (—). Fractions collected for further characterization are denoted by bars and Roman numerals. 

V-1 from acid and alkaline hydrolyzates, SCX-HPLC of amino acids, a mixture of purified crosslinks and hydroxylysine b purified cross-link V-2 c amino acids from an acid hydrolyzate (6 M HCl) of reduced bovine dentin retained on a phenylboronate agarose column after purification as high molecular weight fractions by repeated size exclusion chromatography d as c, alkaline hydrolyzate (2 M KOH). Injections (c, d) resulted from 18 and 52 mg collagen originally hydrolyzed, respectively. 1 = 111 (HP) 2 = V-2 3 = IV 4 = V-1-1 (DHLNL) 5 = HLNL (bovine tendon) 6 = VI (histidinoalanine ) 7 = hydroxylysine 8 = VI (lysinoalanine). 

The occurrence of four collagen cross-links in bovine dentin has been described previously (Linde and Robins, 1988 Walters and Eyre, 1983 Yamauchi et al., 1992) didehydro-hydroxylysinonorleucine (A-HLNL), didehydro-dihydroxylysinonorleucine (A-DHLNL), lysylpyridinoline (LP), and hydroxylysylpyridinoline (HP). In this investigation, only two of these established cross-links were purified HP (peak 111, fig. 1) and DHLNL (peakV-1-1). 

Ranta H (1978) Age-related changes in collagen cross-linking. Changes in bovine dentine and periodontal ligament and description of a new type of non-reducible cross-link. Proc Finn Dent Soc 74 (Suppl. II), 3-64. 

In Chapter 2, the proteolysis of demineralized organic matrix of bovine dentin promoted demineralization of both erosive and subsurface lesions in vitro, especially in advanced lesions. In contrast to previous investigations, the organic matrix was destroyed enzymatically, not chemically. 

Lesion in bovine dentin with tubules protruding from degraded intertubular matrix (left degraded matrix right intact matrix). Demineralization in 0.1 M acetic acid pH 4.0, with subsequent exposure to bacterial collagenase. Fixed and demineralized with glutar-dialdehyde-acetic acid, post-fixed with osmium tetroxide ultrathin sections stained with uranyl acetate - lead citrate. 

Characteristics of demineralized slices of bovine dentin after 4-5 weeks of oral exposure. ... 

Braga RR, Ballester RY, Daronch M. Influence of time and adhesive system on the extrusion shear strength between feldspathic porcelain and bovine dentin. Dental Materials 2000 16(4) 303-310. 

C.M. Amaral, A.R. Peris, G.M. Ambrosano, E.J. Swift Jr., L.A. Pimenta, The effect of light-curing source and mode on microtensile bond strength to bovine dentin, J. Adhes. Dent. 8 (2006) 41 5. 

C.P. Lin, W.H. Douglas, Structure-property relations and crack resistance at the bovine dentin-enamel junction, J. Dent. Res. 73 (1994) 1072-1078. 

P. Wangpermtam, M.G. Botelho, J.E. Dyson, Effect of contamination and decontamination on adhesion of a resin-modified glass-ionomer cement to bovine dentin, J. Adhes. Dent. 13 (2011)445 53. 

R. R. Braga, R. Y. Ballester, and M. Datonch, Influence of Time and Adhesive System on the Extrusion Shear Strength between Feldspathic Porcelain and Bovine Dentin, Dent. Mater., 16, 303-10 (2000). 

S. Phrukkanon, M.E Burrow, P.G. Hartley, M.J. Tyas, The influence of the modification of etched bovine dentin on bond strengths. Dent. Mater, 16, 255-265, 2000. 

MountDuris, G., Silikas. N., and Eliades, G. (2004) Effect of sodium hypochlorite treatment on the molecular composition and morphology of human coronal dentin. /. Adhes. Dent, 6 (3), 175—182. Oook, S. et oL (2004) Influence of polymerization mode of dual-polymerized resin direct core foundation systems on bond strengths to bovine dentin. 

Figu re 6.5 (a) Bovine dentin surface with dentinal tubules covered with E.faecalis bacteria (b) Reduction of viability of E.faecalis bacteria after treatment with nanoparticulate and micron-sized bioactive glass, with nanometric zirconia as an inert reference. Reprinted in part from Refs [60, 61] with permission. 

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