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Biomedical subjects

C Cochet

Publications and source records attributed to C Cochet.

At least 127 records · Page 7Linked to original sources
PubMed1978

[Assignment of alpha-Fuc to1p in man and the chimpanzee and to chromosome 4 in the African green monkey].

Analysis of cellular hybrids confirms the assignment of alpha-L-fucosidase (alpha-FUC) to 1p in man. Discordant results are in favour of the following gene order: 1pter (ENO-1, alpha-FUC,AK2) PGM1 centromere Pep-C but give no information on the relative positions of ENO-1,alpha-FUC, and AK2. The assignments of alpha-FUC to chromosome 1 in the chimpanzee and to chromosome 4 in the African green monkey are demonstrated (chromosome nomenclature by Finaz et al, 1976). These results confirm the homology of chromosome 4 of the African green monkey and 1p of man and the chimpanzee.

Animals↗
PubMed1977

[Regional localization of the genes for human IDHs, MDHs PGK, alphaGAL, G6PD by interspecific hybridization (author's transl)].

22 independent man-hamster (HGPRT-) hybrids using male human cells with balanced reciprocal translocation t(X;2)(p22;q32) were analysed for human genes localized on chromosome 2 (IDHs, MDHs), on chromosome X (PGK, alphaGAL, G6PD) and for the different chromosomes in relation with the balanced reciprocal translocation (chr.2, chr.2q-, chr.Xp+). The following results were obtained: The chromosomes 2 and 2q- are absent in the 22 hybrids. In 9 hybrids, the absence of MDHs in spite of the presence of the chromosome Xp+ indicates that the gene for MDHs is not localized on this chromosome (or that the gene for MDHs is not on the segment 2q32--2qter translocated on X). In 14hybrids, the three markers of X (PGK, alphaGAL, G6PD) and IDHs are expressed in the presence of the chromosome Xp+. This result indicates that the genes for these markers are on Xp+ or that the genes PGK, alphaGAL, G6PD are on X without the Xp22--Xter segment, translocated on the chr.2, and that the gene for IDHs is on the 2q32--2qter segment translocated on X. In 8 hybrids, in the absence of the intack chromosome Xp+, the higher percentage of the presence of G6PD (7 hybrids) and the lower percentage of the presence of IDHs (3 hybrids) are explained by the fact that these hybrids selected in HAT medium had to retain a segment of Xp+ bearing the human gene HGPRT. G6PD appeared very close to HGPRT and IDHs very distant from HGPRT. The study of the different correlations between the presence and the absence of these four markers on Xp+ in the different hybrids indicates the following order on the chromosome Xp+ from p to q: IDHs -- PGK --alphaGAL -- G6PD.

Animals↗
PubMed1977

[Demonstration of high affinity binding of estradiol in adrenal cortex tissue].

Evidence is presented demonstrating the presence of a high affinity (Ka10(8)M-1), limited capacity (3-4 pmoles/mg protein) estradiol binder in the soluble fraction of the Bovine, Rat and Human adrenal cortex. The binding appears specific to the estrogen structure whereas C19 and C21 steroids do not bind. Upon sucrose density gradient centrifugation, the estradiol binder sedimented at 9 S at low ionic strength and was shifted to 4.5 S in the presence of 0.5 M KCl. This demonstration of a receptor-like moiety for estradiol in the adrenal cortex lends biochemical support to previous observations suggesting that adrenal cortex functions may be modulated by a direct effect of gonadal steroid hormones.

Adrenal Cortex↗
PubMed1976

Glucocorticoid binding in the chicken liver cytosol. Characterization of five macromolecular binding components.

The heterogeneity of the glucocorticoid binding in the chicken liver cytosol, previously suggested by the results obtained with crude preparations, was confirmed using different techniques such as stepwise ammonium sulfate precipitation, hydroxyapatite chromatography and gel filtration on Sephadex G-200. The latter method permitted the separation of five glucocorticoid binding macromolecules respectively named binders S1, S2, S3, S4 and S5, according to their decreasing apparent molecular size upon gel filtration. Apparent molecular weight, binding affinity, capacity and specificity of these five moieties were examined. In addition, S-aryl-transferase activity using glutathione as co-substrate was studied and found to coincide mostly with the fractions containing binder S4, which might represent an avian liver ligandin.

Animals↗