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Biomedical subjects

C Thibault

Publications and source records attributed to C Thibault.

At least 73 records · Page 4Linked to original sources
PubMed1985

Variation of astigmatism with accommodation and its relationship with dark focus.

The refraction of 122 eyes was measured for five distances of fixation with an objective Canon Auto Refractor. The cylindrical component was found to vary, but by a small amount. We found no evidence of a deliberate reduction in astigmatism with accommodation, in accord with other studies. The axis was also found to vary by at least 5 degrees in about half of the subjects tested, which is also in good accord with other investigations. The dark focus of 31 eyes was not found to correlate with a minimum astigmatic distance, since this only occurred in 11 out of the 31 eyes. For these 11 eyes, the correlation of dark focus and the dioptric distance where astigmatism was minimum was equal to + 0.54. It implied that for those eyes (about one-third of all types) there was a tendency to yield the best optical quality at the dark focus.

Accommodation, Ocular↗
PubMed1984

Insulin-like growth factor II receptors. Molecular radius and molecular weight determination using quantitative polyacrylamide gel electrophoresis.

High resolution quantitative polyacrylamide gel electrophoresis was employed under nondenaturing conditions to calculate a molecular weight, Mr, for rat placental membrane receptors that bind insulin-like growth factor II (IGF-II). An n-octylglucoside-soluble extract of receptors that had been enriched 20-fold during Sephacryl S-300 gel chromatography and designated peak 1 (Perdue, J. F., Chan, J. K., Thibault, C., Radaj, P., Mills, B., and Daughaday, W. H. (1983) J. Biol. Chem. 258, 7800-7811) was incubated with 125I-IGF-II in the presence or absence of an excess of unlabeled IGF-II and electrophoresed in glass tubes containing highly cross-linked polyacrylamide gels at concentrations ranging from 5 to 12% (w/v). A specifically labeled peak of IGF-II binding activity was identified by freezing, slicing, and counting the gels. The proteins eluted from the region of the gel when cross-linked to 125I-IGF-II with disuccinimidyl suberate and electrophoresed in the presence of sodium dodecyl sulfate have the same molecular weight, Mr, as the previously described IGF-II receptor. From the slope of a plot of log of the relative mobility, RF, at each of 6 to 7 gel concentrations for the 125I-IGF-II-receptor and for each of seven standard proteins (Ferguson-Hedrick plot), a retardation coefficient, KR, was determined. Using a reference curve constructed from a plot of square root KR versus the molecular radius, R, of the standard proteins, the IGF-II receptor was estimated to have a R of 4.13 nm and a calculated Mr of 250,000. Thus, quantitative procedures that separate native proteins based on their size and charge have provided information which is in good agreement with the results of studies of the IGF-II-receptor by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and supports the premise that it is a monomeric single chained glycoprotein, constrained by intradisulfide bonds and with a mass of 250 kDa.

Animals↗
PubMed1983

The biochemical characterization of detergent-solubilized insulin-like growth factor II receptors from rat placenta.

A membrane preparation, the R3, obtained by differential centrifugation of rat placental homogenates is enriched in receptors that bind insulin-like growth factor II (IGF-II) preferentially and with avidity (Daughaday, W.H., Mariz, I.K., and Trivedi, B. (1981) J. Clin. Endocrinol. Metab. 53, 282-288). When this preparation was incubated with 2% (w/v) octyl-beta-D-glucopyranoside for 60 min at 0-4 degrees C, 60% of the membrane protein was solubilized without loss of binding activity. The 125I-IGF-II binding properties of the detergent-solubilized receptors were found to be similar to those of the membrane-associated receptor. The rate constants for association, ka, and dissociation, kd, and equilibrium dissociation constant, KD, were 8.5 X 10(8) M-1 min-1, 7.5 X 10(-3) min-1, and 1.3 nM for the detergent-solubilized receptors and 5.3 X 10(8) M-1 min-1, 4.2 X 10(-3) min-1, and 0.6 nM for the membrane receptors. Gel chromatography on Sephacryl S-300 concentrated the solubilized receptors into a major peak of binding activity with a Stokes radius of 7.2 nm; a second peak of less specific binding had a Stokes radius of 4.3 nm. The receptors in the major peak bound 125I-IGF-II with a KD of 0.6 nM; the total binding capacity, Ro, was 21.6 pmol mg of protein-1 compared to 1.6 pmol mg of protein-1 for the membrane-associated receptor. Centrifugation of the receptors on 5-20% (w/v) gradients of sucrose in H2O or D2O disclosed a heterogeneous pattern of receptor distribution. When they were labeled with 125I-IGF-II prior to centrifugation, a major form of the receptor with a sedimentation constant, S20,w, of 9.9 X 10(13) s and other, possibly smaller, forms of the receptor were observed. However, only the 9.9 s20,w form of the receptor was observed if it was labeled with 125I-IGF-II subsequent to centrifugation. Based on these hydrodynamic measurements and a partial specific volume of 0.72 cm3/g, the IGF-II receptor was calculated to have a Mr of 290,000 and frictional ratio, f/fo, of 1.6. This value for the Mr is similar to the mass of 220,000 or 250,000 Dal determined by cross-linking 125I-IGF-II to the membrane- or detergent-solubilized receptors with disuccimidyl suberate and separating the complex by electrophoresis in sodium dodecyl sulfate-containing polyacrylamide gels in the absence or presence of dithiothreitol, respectively.

Animals↗
PubMed1976

[Culture of the bovine graafian follicle in a continuous liquid and gas flow system].

The culture of 3-5 mm calf follicles in a new glass perfusion cell is compared to the organotypic grid culture using the same synthetic medium and a gas mixture of 55% O2 + 40% N2 and 5% CO2 Amino acid consumption is 3 to 39 times higher in the perfusion cell culture and the mitotic rate is also higher. Moreover, the cytological aspect of granulosa and cumulus cells looks similar to that of non-atresic ovarian follicles. Meiosis resumes up to metaphase 1 or metaphase 2. No pyknotic cells are observed.

Air↗
PubMed1975

Preovulatory and ovulatory mechanisms in oocyte maturation.

Studies of the effect of gonadotrophins on the cumulus and oocyte or on the whole follicle in vitro offer a good tool for understanding the mechanisms of oocyte maturation, the ability of follicles of different sizes to respond to gonadotrophins and the processes of atresia. The birth of normal young from intrafollicular oocytes matured in vitro furnishes proof that in-vitro techniques are valuable as long as follicular integrity is maintained during the whole culture period.

Animals↗