Search

Your search keyword '"Dautrevaux M"' showing total 273 results
Start Over Author "Dautrevaux M"
273 results on '"Dautrevaux M"'

1. Évaluation de l’impact d’une formation pluriprofessionnelle au repérage et l’accompagnement des femmes victimes de violences conjugales en soins de santé primaires en Meuse

Author

Audrey Ronchi, Laurent MARTRILLE, Dautrevaux, M., Paolo Di Patrizio, Olivier Bouchy, Di Patrizio, Paolo, and Université de Lorraine (UL)

Subjects
[SDV.EE.SANT]Life Sciences [q-bio]/Ecology, environment/Health, [SDV.EE.SANT] Life Sciences [q-bio]/Ecology, environment/Health, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2019

14. Structural Analysis of the Glycine-Rich, Arginine-Rich Histone form Calf Thymus: The Tryptic Peptides.

Author

Nautière, P., Moschetto, Y., Dautrevaux, M., and Biserte, G.

Subjects
HISTONES, THYMUS, CALVES, AMINO acids, ARGININE, BIOCHEMISTRY
Abstract

The gycine-rich, arginine-rich histone from calf thymus contains 102 residues of amino acids, distributed as follows: Asp5, Thr7, Ser2, Glu6, Pro1, Gly17,. Ala7, Val9, Met1, Ile6, Leu8, Tyr4, Phe2, Lys10, Lys(Me)1, His2, Arg14. From a tryptic hydrolysate of Gly- and Arg-rich histone, 18 peptides were isolated by fractionation on a column of Chromobeads P followed by purification by paper electrophoresis and chromatography. The amino acid compositions of these peptides are reported. The sequence of 12 of these tryptic peptides has been established. The amino-terminal tryptic peptide is Ac-Ser-Gly-Arg. The carboxylterminal tryptic peptide is Thr-Leu-Tyr-Gly-Phe-Gly-GlyCOOH. [ABSTRACT FROM AUTHOR]

Published
1970

15. Structure covalente de la myoglobine de cheval

Author

Dautrevaux M, Biserte G, Boulanger Y, and Kia-Ki Han

Subjects
chemistry.chemical_classification, Chymotrypsin, Edman degradation, biology, Peptide, Biochemistry, chemistry.chemical_compound, Myoglobin, chemistry, biology.protein, Peptide bond, Cyanogen bromide, Globin, Peptide sequence
Abstract

The complete sequence (153 amino acids) of horse heart myoglobin has been established. The sequence of a peptide isolated from chymotrypsin hydrolyzates of globin allowed to fill a gap in the tentative sequence previously proposed; this peptide was studied by means of pepsin hydrolysis, action of N-bromosuccinimide on histidyl bonds, and Edman degradation method associated with dansylation. After hydrolysis of globin by chymotrypsin treated by TLCK, the same major peptides were found as after hydrolysis by non-treated chymotrypsin. These peptides were identified by ion-exchange resins and bidimensional paper chromatography, and also by the determination of their amino-acid composition. The suppression of secondary cuts explains the presence of new peptides, whose the composition and N-terminal sequences were determined. It was then possible to confirm several sequences which could be previously deduced from the study of split products after cyanogen bromide treatment. The specificity of chymotrypsin towards certain types of peptide bonds is discussed. Horse myoglobin, as compared with sperm whale myoglobin, contains 18 differences: 17 substitutions and one inversion. The major part of the substitutions are located in N- and C-terminal sequences; they are all punctiform, resulting from the replacement of only one base in each codon.

Published
1969
Full Text
View/download PDF

20. RNA binding to the untransformed glucocorticoid receptor. Sensitivity to substrate-specific ribonucleases and characterization of a ribonucleic acid associated with the purified receptor.

Author

UCL - MD/BICL - Département de biochimie et de biologie cellulaire, Sablonnière, B, Economidis, I V, Lefebvre, P., Place, M., Richard, C., Formstecher, P., Rousseau, Guy, Dautrevaux, M, UCL - MD/BICL - Département de biochimie et de biologie cellulaire, Sablonnière, B, Economidis, I V, Lefebvre, P., Place, M., Richard, C., Formstecher, P., Rousseau, Guy, and Dautrevaux, M

Abstract

The cytosolic untransformed molybdate-stabilized glucocorticoid-receptor complex from rat liver was eluted as a heterogenous peak containing two components with Stokes radii (Rs) of 8.3 nm and 7.1 nm when analyzed by size-exclusion HPLC even in the absence of molybdate. In contrast, the highly purified glucocorticoid receptor yielded a sharp symmetrical peak of Rs = 7.1 nm. We demonstrate that the 7.1-nm component could not result from a proteolytic degradation of the 8.3-nm receptor form. The same receptor heterogeneity was observed in thymus cytosol which contains less proteases than liver. After labeling with [3H]dexamethasone 21-mesylate and SDS/PAGE the same 94-kDa receptor band was revealed in both the 8.3-nm and 7.1-nm forms. Immunoblotting experiments showed that both the 94-kDa hormone-binding subunit and the 90-kDa heat-shock protein were present in the two different receptor forms. The 8.3-nm receptor form was converted to the 7.1-nm receptor form after treatment by ribonuclease A in the presence of molybdate and this effect was dose-dependent, being completely prevented by placental ribonuclease inhibitor (RNasin). In contrast, in the presence of molybdate, the 7.1-nm receptor form was ribonuclease-insensitive. Treatment of cytosol with RNase A in the absence of molybdate, partially shifted the untransformed receptor towards the 5.2-nm transformed receptor form. This effect was abolished by placental ribonuclease inhibitor. RNase S protein, an enzymatically inactive proteolytic fragment of RNase A, or S1 nuclease, which is specific for single-stranded nucleic acids, were ineffective when used instead of RNase A. In contrast, cobra venom endonuclease, which preferentially attacks double-stranded regions of small RNAs, caused a complete conversion of the 7-8-nm untransformed receptor to the 5.2-nm transformed receptor form. These results were not observed in the presence of molybdate. Addition of RNasin prior to heating cytosol in the absence of molybdate

Published
1988

21. Improvement in glucocorticoid receptor binding affinity concomitant to shift from antagonist to agonist activity in a series of 17 beta-carboxamide derivatives of dexamethasone.

Author

UCL - MD/BICL - Département de biochimie et de biologie cellulaire, Lefebvre, P., Formstecher, P., Rousseau, Guy, Lustenberger, P, Dautrevaux, M, UCL - MD/BICL - Département de biochimie et de biologie cellulaire, Lefebvre, P., Formstecher, P., Rousseau, Guy, Lustenberger, P, and Dautrevaux, M

Abstract

Modification of the 17 beta-side chain of the synthetic glucocorticoid agonist dexamethasone by periodic oxidation and subsequent coupling to various primary amines yield secondary 17 beta-carboxamide derivatives displaying antiglucocorticoid activity in vitro, but not in vivo. To obtain more potent antiglucocorticoids, new secondary and tertiary 17 beta-carboxamide derivatives were synthesized. Although they displayed an improved affinity for the glucocorticoid receptor in rat thymus cytosol and antiglucocorticoid activity in rat hepatoma (HTC) cells, these new compounds were again devoid of in vivo antiglucocorticoid activity in the rat. Moreover, the increase in receptor binding affinity was correlated for most compounds with the appearance of a partial agonist activity in HTC cells. The tertiary 17 beta-carboxamide derivative DX diMe displayed the highest affinity but was also a partial agonist in vivo. Kinetic studies with several tritiated 17 beta-carboxamide derivatives showed that they had association rate constants similar to that of dexamethasone, but different dissociation rate constants. The rapid dissociation of the compounds displaying antiglucocorticoid activity contrasted with the slow dissociation of DX diMe. Therefore, antiglucocorticoid activity in the 17 beta-carboxamide series is probably related to the formation of rapidly dissociating glucocorticoid receptor-ligand complexes that are unable to undergo the transformation step.

Published
1989

22. Structural analysis of the glycine-rich, arginine-rich histone from calf thymus: the tryptic peptides

Author

Y Moschetto, Gérard Biserte, Dautrevaux M, and Pierre Sautiere

Subjects
Electrophoresis, Arginine, Chromatography, Paper, Glycine, Thymus Gland, Buffers, Biochemistry, Hydrolysate, Histones, medicine, Animals, Trypsin, Amino Acid Sequence, Amino Acids, Peptide sequence, chemistry.chemical_classification, Chromatography, integumentary system, biology, Chemistry, Chromatography, Ion Exchange, Amino acid, Histone, biology.protein, Cattle, Peptides, medicine.drug
Abstract

The glycine-rich, arginine-rich histone from calf thymus contains 102 residues of amino acids, distributed as follows: Asp5, Thr7, Ser2, Glu6, Pro1, Gly17, Ala7, Val9, Met1, Ile6, Leu8, Tyr4, Phe2, Lys10, Lys(Me)1, His2, Arg14. From a tryptic hydrolysate of Gly- and Arg-rich histone, 18 peptides were isolated by fractionation on a column of Chromobeads P followed by purification by paper electrophoresis and chromatography. The amino acid compositions of these peptides are reported. The sequence of 12 of these tryptic peptides has been established. The amino-terminal tryptic peptide is Ac-Ser-Gly-Arg. The carboxylterminal tryptic peptide is Thr-Leu-Tyr-Gly-Phe-Gly-GlyCOOH.

Published
1970

23. Guanidination of horse heart myoglobin

Author

Kia-Ki Han, Boulanger Y, Biserte G, and Dautrevaux M

Subjects
chemistry.chemical_compound, Biochemistry, Myoglobin, chemistry, Structural Biology, Genetics, Biophysics, Horse, Cell Biology, Molecular Biology
Published
1969

Catalog

Books, media, physical & digital resources
See catalog results