13 results match your criteria: "Centre de Recherche de Biologie et Physico-Chimie Cellulaires[Affiliation]"
Biochim Biophys Acta
October 1997
Laboratoire de Biochimie, UPRES 2161, Centre de Recherche de Biologie et Physico-chimie Cellulaires, Faculté des Sciences et des Techniques, Nantes, France.
An acid beta-galactosidase was isolated from the digestive juice of Achatina achatina and purified to homogeneity by anion exchange, gel-filtration and hydroxyapatite chromatographies. This enzyme is soluble, as are the cytosolic beta-galactosidases, functions at acid pH like the lysosomal enzymes but differs from the other soluble animal beta-galactosidases in that it is highly specific for the beta-D-galactosyl residue. In addition, it cleaves the beta1-4 linkage much faster than the beta1-3 and beta1-6 linkages.
View Article and Find Full Text PDFInt J Biochem Cell Biol
May 1996
Laboratoire de Biochimie, Faculté des Sciences, Centre de Recherche de Biologie et Physico-Chimie Cellulaires, Nantes, France.
The G2 form of butyrylcholinesterase (BChE) of mucosal cells of rat intestine is a rare amphiphilic species, which is related to class II of acetylcholinesterase. Preliminary work indicated that the enzyme can bind heparin and suggested particular properties as compared to other BChEs. Ionic properties of the G2 form BChE were studied with different ionic exchangers.
View Article and Find Full Text PDFBiochemistry
November 1992
Laboratoire de Biochimie II, Faculté des Sciences, Centre de Recherche de Biologie et Physico-Chimie Cellulaires, Nantes, France.
The properties of a cholinesterase from mucosal cells of rat intestine have been characterized. The enzyme was identified as butyrylcholinesterase because it was more sensitive to iso-OMPA (IC50 = 1.0 x 10(-6) M) than to BW284C51 (IC50 = 5.
View Article and Find Full Text PDFMol Cell Biochem
April 1991
Laboratoire de Biochimie II, Centre de Recherche de Biologie et Physico-Chimie Cellulaires, Nantes, France.
The butyrylcholinesterase activity of chick enterocytes was studied from day 15 in ovo up to day 90 after hatching. The activities detected in both sexes at the level of jejuno-ileum change in a parallel manner, but the activity is always higher in the female than in the male during embryonic development. After hatching, the differences are less apparent although the study of the enzyme distribution along the intestine showed sex-related variations, mainly at the level of the anterior and middle parts of jejuno-ileum in the young adult.
View Article and Find Full Text PDFMol Cell Biochem
August 1990
Laboratoire de Biochimie II, Centre de Recherche de Biologie et Physico-Chimie Cellulaires, Nantes, France.
The mucosal cells of the chicken intestine contain a cholinesterase activity essentially due to butyrylcholinesterase. The enzyme is present during embryonic and post-hatching development. The activity reaches a maximum value at day 19 in ovo and decreases prior to and after hatching up to day 4 ex ovo.
View Article and Find Full Text PDFJ Neurochem
March 1990
Groupe de Physiologie Cellulaire, Centre de Recherche de Biologie et Physico-Chimie Cellulaires, Faculté des Sciences, Nantes, France.
The effects of denervation and direct electrical stimulation upon the activity and the molecular form distribution of butyrylcholinesterase (BuChE) were studied in fast-twitch posterior latissimus dorsi (PLD) and in slow-tonic anterior latissimus dorsi (ALD) muscles of newly hatched chicken. In PLD muscle, denervation performed at day 2 substantially reduced the rate of rapid decrease of BuChE specific activity which takes place during normal development, whereas in the case of ALD muscle little change was observed. Moreover, the asymmetric forms which were dramatically reduced in denervated PLD muscle were virtually absent in denervated ALD muscle at day 14.
View Article and Find Full Text PDFDifferentiation
August 1989
Centre de Recherche de Biologie et Physico-Chimie Cellulaires, Faculté des Sciences et des Techniques, Nantes, France.
The accumulation of acetylcholinesterase (AChE), the changes in AChE-specific activity and in AChE molecular form distribution were studied in slow-tonic anterior latissimus dorsi (ALD) and in fast-twitch posterior latissimus dorsi (PLD) muscles of the chick embryo. From stage 36 (day 11) to stage 42 (day 17) of Hamburger and Hamilton, the AChE-specific activity decreased, while the relative proportion of asymmetric A 12 and A 8 forms increased. Repetitive injection of curare resulted at stage 42 (day 17) in a decrease in AChE-specific activity, in the accumulation of the synaptic AChE and in the expression of AChE asymmetric forms.
View Article and Find Full Text PDFDevelopment
June 1989
Groupe de Physiologie Cellulaire, Centre de Recherche de Biologie et Physico-Chimie Cellulaires, Faculté des Sciences, Nantes, France.
Slow-tonic anterior latissimus dorsi (ALD) muscle properties were studied following chronic spinal cord stimulation in chick embryo. Stimulation at a fast rhythm was applied from day 7, 8 or 10 of development until the end of embryonic life. When stimulation was applied from day 7 up to day 18 of development, ALD muscle exhibited at day 18 a large decrease in half time to peak of tetanic contraction, a large proportion of fast type II fibres and an increase in fast myosin light chain content as compared to control muscle.
View Article and Find Full Text PDFMol Cell Biochem
January 1989
Laboratoire de Biochimie II, Centre de Recherche de Biologie et Physico-Chimie Cellulaires, Faculté des Sciences, Nantes, France.
The presence of a butyrylcholinesterase (BuChE, EC 3.1.1.
View Article and Find Full Text PDFBiochimie
January 1989
Laboratoire de RMN et Réactivité Chimique, UA CNRS no. 472, Centre de Recherche de Biologie et Physico-Chimie Cellulaires, Nantes, France.
The binding of Ca2+ to membrane models composed of diplamitoylphosphatidylcholine (DPPC) and dipalmitoylphosphatidylethanolamine (DPPE) 15N-labeled in the polar head group was investigated at pH 8.5 and pH 9.4 by 15N-NMR spectroscopy.
View Article and Find Full Text PDFDifferentiation
November 1988
Centre de Recherche de Biologie et Physico-Chimie Cellulaires, Faculté de Sciences, Nantes, France.
The evolution of acetylcholinesterase (AChE) activity and AChE molecular form distribution were studied in slow-tonic anterior latissimus dorsi (ALD) and in fast-twitch posterior latissimus dorsi (PLD) muscles of chickens 2-18 days of age. In ALD as well as in PLD muscles, the AChE-specific activity increased transiently from day 2 to day 4; the activity then decreased more rapidly in PLD muscle. During this period asymmetric AChE forms decreased dramatically in ALD muscle and the globular forms increased.
View Article and Find Full Text PDFReprod Nutr Dev (1980)
November 1988
Groupe de Physiologie Cellulaire, Centre de Recherche de Biologie et Physico-Chimie Cellulaires, Faculté des Sciences, Nantes, France.
The fast posterior latissimus dorsi muscle (PLD) of the chick ceases to accumulate slow myosin light chains (MLC) during neonatal development. On day 18 of embryonic life slow MLC represented only 2% of total MLC, and LC3F was first detected. In chick embryo, spinal cord stimulation at a slow rhythm modifies PLD differentiation toward the slow type: LC3F did not accumulate and slow MLC increased.
View Article and Find Full Text PDFPflugers Arch
November 1987
Groupe de Physiologie Cellulaire, Centre de Recherche de Biologie et Physico-Chimie cellulaires, Faculté des Sciences, Nantes, France.
The effects of denervation and direct stimulation in fast and slow latissimus dorsii muscles were investigated in chicken. In slow ALD muscle, denervation resulted in an incompleteness of the relaxation, a decrease in MDH and CPK activities and an increase in fast myosin light chains (MLC) accumulation. Direct stimulation at either fast or slow rhythm prevented the effects of denervation on relaxation and CPK activity but was ineffective on MDH activity and fast MLC accumulation.
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