Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Jean-Jacques Bechet"'
Autor:
Anne Ozog, Jean-Jacques Bechet
Publikováno v:
European Journal of Biochemistry. 234:501-505
The far-ultraviolet circular dichroism and fluorescence emission intensities of the myosin rod were studied at pH 2-11, in the absence and presence of guanidine hydrochloride. The protein kept its helicity in this pH range. Its stability in the denat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a042c45b424f62f40743f9b5ad1be30
https://doi.org/10.1111/j.1432-1033.1995.501_b.x
https://doi.org/10.1111/j.1432-1033.1995.501_b.x
Publikováno v:
European Journal of Biochemistry. 207:951-955
Myosin and creatine kinase were co-immobilized onto Immunodyne films to mimic the behaviour of creatine kinase bound to the M-line of myofilaments. The Mg-ATPase activity of bound myosin was studied by a coupled enzymatic assay, which detects Mg-ADP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e76874aabceacfbfb52e9c10e132860c
https://doi.org/10.1111/j.1432-1033.1992.tb17129.x
https://doi.org/10.1111/j.1432-1033.1992.tb17129.x
Publikováno v:
Biochemistry. 31:1210-1215
The effect of guanidine hydrochloride on ATPase activity, gel filtration, turbidity, exposure of thiol groups, far-UV circular dichroism, and the fluorescence emission intensity of myosin subfragment 1 (S-1) was studied under equilibrium conditions.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcc5540d3e47415542b4d54536e16f41
https://doi.org/10.1021/bi00119a034
https://doi.org/10.1021/bi00119a034
Autor:
Georges Foucault, Anne-Marie Lompré, Sophie Quevillon-Cheruel, Michel Desmadril, Jean-Jacques Bechet
Publikováno v:
FEBS letters. 454(3)
The two light meromyosin isoforms from rabbit smooth muscle were prepared as recombinant proteins in Escherichia coli. These species which differed only by their C-terminal extremity showed the same circular dichroism spectra and endotherms in measur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25ba206c4f41a47ee9e412d2e5ac9ad7
https://pubmed.ncbi.nlm.nih.gov/10431827
https://pubmed.ncbi.nlm.nih.gov/10431827
Publikováno v:
European journal of biochemistry. 191(3)
Several structural and enzymatic properties of myosin from skeletal muscles of neonatal and adult rabbits were compared. Electrophoretic analyses and proteolysis experiments indicated that differences between the two myosin types could be attributed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4563ba5ac5ec47b52eb024cc11f45dbe
https://pubmed.ncbi.nlm.nih.gov/2143987
https://pubmed.ncbi.nlm.nih.gov/2143987
Publikováno v:
European Journal of Biochemistry. 156:291-296
Adult rat, mouse, and guinea-pig masseter muscles display distinct myosin electrophoretic patterns. The rat muscle contains four main forms which by reference to the myosins of the IIB tensor fasciae latae, of the IIA mylohyoid, and of the red and wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37e2d405184bf534903b1cb9776e4824
https://doi.org/10.1111/j.1432-1033.1986.tb09580.x
https://doi.org/10.1111/j.1432-1033.1986.tb09580.x
Publikováno v:
Biochemistry. 18:4080-4089
The hydrolysis of Mg2+-adenosine 5'-triphosphate (ATP) by heavy meromyosin has been studied between +20 and -15 degrees C, especially in the low-temperature range, in a medium containing 30% (v/v) ethylene glycol by fluorometric, spectrophotometric,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e952806fa3a069a7e9e2c02efca4414c
https://doi.org/10.1021/bi00586a004
https://doi.org/10.1021/bi00586a004
Publikováno v:
Biochimie. 64:399-404
The myosin isoenzymic content of several adult rat muscles has been analyzed by electrophoresis under non-dissociating conditions. Fast-twitch fibres, whether of the oxidative type, such as the red masseter, or of the glycolytic type, such as the whi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::336f868d621556f5310004d775141b5a
https://doi.org/10.1016/s0300-9084(82)80577-4
https://doi.org/10.1016/s0300-9084(82)80577-4
Publikováno v:
European Journal of Biochemistry. 161:343-349
The number of active sites of soluble and filamentous myosin and of its subfragments, heavy meromyosin and subfragment-1, has been determined. The titration involves steady-state kinetic measurements at a high enzyme concentration and varying substra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ede98ea345093fc84269d5ed89f01f5d
https://doi.org/10.1111/j.1432-1033.1986.tb10453.x
https://doi.org/10.1111/j.1432-1033.1986.tb10453.x
Autor:
Jean-Jacques Bechet
Publikováno v:
Journal de Chimie Physique. 61:584-591
L’etude cinetique et thermodynamique de l’hydrolyse trypsique du p-toluene-sulfonyl-L-arginine methylester, aux faibles concentrations de substrat, montre que deux groupements de la trypsine, dont les pK d’ionisation sont respectivement 7,5 et
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5bc71219875d0b3e9239222bd169ff89
https://doi.org/10.1051/jcp/1964610584
https://doi.org/10.1051/jcp/1964610584