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1.
Caries Res ; 26(3): 170-5, 1992.
Article in English | MEDLINE | ID: mdl-1628290

ABSTRACT

The crowns of 60 permanent human molars were sectioned transversally. The exposed dentin surface was divided into different parts: a first part was kept as control, a second part was immediately varnished, and a third part was irradiated with a CO2 laser using the same irradiation conditions as those applied for caries removal (10 impulses of the same energy; 0.2 s/impulse; energy density/impulse 280-715 J/cm2. After irradiation, a small portion of this area was varnished. The teeth were immersed for 4 weeks in a cariogenic gel (pH = 4.5) at 36 degrees C. Twenty teeth were studied by scanning electron microscopy, and longitudinal sections of the other teeth were prepared for microradiography and microdensitometry measurements. The lased dentin surface appeared smooth for energy densities lower than 425 J/cm2. Longitudinally fractured samples revealed a layer of dentin devoid of tubular structure (20-70 microns thick, depending on the energy density used), whereas below the sealed layer, the dentinal tubules retained their normal aspect. Although the sealed layer showed no demineralization when exposed to acid, demineralization of the underlying dentin occurred, but to a much lesser extent than in the unlased dentin.


Subject(s)
Dental Caries/prevention & control , Dentin/radiation effects , Laser Therapy , Carbon Dioxide , Densitometry , Dentin/chemistry , Dentin/ultrastructure , Humans , Lactates , Lactic Acid , Microradiography , Microscopy, Electron, Scanning , Minerals/analysis , Molar , Pit and Fissure Sealants , Tooth Demineralization/prevention & control
2.
J Biol Buccale ; 17(3): 179-86, 1989 Sep.
Article in English | MEDLINE | ID: mdl-2808333

ABSTRACT

In order to weld cracks in tooth enamel, it is necessary to bring the surface of the tooth to the fusion temperature of the enamel (greater than 1,000 degrees C). The study investigated whether this increase in surface temperature can cause damage to the vitality of the tooth by recording, using a thermocouple, the temperature in the pulp chamber of teeth exposed to argon laser irradiation (power density after focusing: 4000 W/cm2; duration of continuous irradiation: 1-5 seconds). These pulp temperature increases were compared with those considered safe for the tooth, i.e., contact with a hot drink, drilling of cavities with air + water cooling. It was shown that punctual irradiations with an argon laser for periods of 2 or 4 seconds generated temperature increases in the pulp chamber which were less than inferior to those caused by contact with water at 54-55 degrees C for 1 or 2 seconds, and were of the same order as those caused by the drilling of class III or V cavities of 1 mm in depth and 1 mm in diameter. These results suggest that it is worth continuing research into applying the technique in the mouth.


Subject(s)
Body Temperature , Cuspid/physiology , Dental Cavity Preparation , Dental Pulp/physiology , Hot Temperature , Lasers , Humans , In Vitro Techniques , Tooth Fractures/therapy , Welding
3.
J Biol Buccale ; 15(1): 37-43, 1987 Mar.
Article in English | MEDLINE | ID: mdl-3470288

ABSTRACT

An all line argon laser beam of initial power 2W (4000W/cm2-800 J/cm2, after focusing), was used to weld enamel cracks on extracted human teeth. The welding, observed with the naked eye, caused a small heightening in the welded area which was whiter in color than the rest of the enamel. Examinations were performed on the outer surface of the welding with an inverted metallurgical microscope and using a microdurometer. Sections were then made and studied, on the one hand with a light microscope, and on the other using microradiographical methods. The welding was seen to reach across half the enamel thickness. The possibilities for therapeutic applications of this work are discussed.


Subject(s)
Dental Enamel/injuries , Laser Therapy , Tooth Fractures/therapy , Argon , Dental Enamel/pathology , Hardness , Humans , Tooth Fractures/pathology
4.
J Mol Biol ; 181(2): 317-22, 1985 Jan 20.
Article in English | MEDLINE | ID: mdl-3884821

ABSTRACT

Isolated insulin monomers, the dimer and higher aggregates from the 2 Zn crystal structure are subjected to convergent energy minimization in Cartesian co-ordinates using a force-field that includes the position of all hydrogen atoms. The minimizations are found, for the first time, to produce conformational changes of appreciable magnitude, which agree well with observed structural differences between monomers in the 2 Zn crystal and with the mechanism proposed previously for the coupling between deformations in different parts of the molecule. Our results also suggest that insulin would tend to adopt a molecule 1-like conformation in the absence of crystal packing forces, and that dimer formation is not at the origin of the observed asymmetry in the 2 Zn crystal.


Subject(s)
Insulin , Computers , Crystallization , Macromolecular Substances , Protein Conformation , Zinc
5.
Int J Pept Protein Res ; 15(1): 41-53, 1980 Jan.
Article in English | MEDLINE | ID: mdl-6987188

ABSTRACT

The insulins of pig, ox, horse and goat differ only by the cyclic A6-A11 peptide which is thought to be an antigenic determinant of the molecule. The structure of the four peptides is investigated by conformational energy calculations in order to verify whether a common backbone conformation can be found for all four species, the antigenic difference being consequently due only to the difference in the side chains exposed to the solvent, or whether each sequence gives rise to a preferential backbone conformation, which would lead to the conclusion that the antigenic difference is conveyed by a more pronounced difference in the molecular structure. From the results of the study on the isolated peptides, it appears that an energetically favourable backbone conformation common to all four species can be found. This conformation is compared with the structure deduced from the X-ray diffraction data available for pig insulin.


Subject(s)
Insulin , Amino Acid Sequence , Animals , Cattle , Goats , Horses , Peptide Fragments , Protein Conformation , Species Specificity , Swine , X-Ray Diffraction
9.
FEBS Lett ; 2(4): 233-235, 1969 Feb.
Article in French | MEDLINE | ID: mdl-11946320

ABSTRACT

It is well known that, in rabbits, the allotypes of the b locus carried by the light chains of the IgG molecules cross-react. Nothing similar has been described for the allotypes of the a locus carried by the heavy chains of the IgG molecules. This paper describes a cross-reaction between the rabbit allotypic markers Aa1 and Aa2 of the a locus. This phenomenon became evident in successive I(125)-labelled IgG precipitation experiments with a particular serum.

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