Zobrazeno 1 - 10
of 57
pro vyhledávání: '"J.P. Le Caer"'
Autor:
J.P. Le Caer, Laure Béven, Joël Chopineau, Hervé Adenier, Virginie Redeker, R Kichenama, Johanne Homand, Daniel Ladant
Publikováno v:
Biochemistry. 40:8152-8160
Neurocalcin is a member of a novel family of neuronal calcium sensors that belongs to the superfamily of EF-hand Ca(2+)-binding proteins. Neurocalcin is myristoylated on its N-terminus in vivo and can associate with biological membranes in a calcium
Publikováno v:
Analusis. 26:22-25
Publikováno v:
Biochimie. 79:731-740
Cysteinyl-tRNA synthetase (CRS) from Saccharomyces cerevisiae was purified 2300-fold with a yield of 33%, to high-specific activity (kcal4.3 s−1 at 25°C for the aminoacylation of yeast tRNACys). SDS-PAGE revealed a single polypeptide corresponding
Autor:
Jérôme Rossier, Mehrnaz Katouzian-Safadi, B. Blazy, Jean-Yves Cremet, J.P. Le Caer, Michel Charlier
Publikováno v:
Biochemistry. 32:1770-1773
Adenosine cyclic 3',5'-phosphate receptor protein (CRP or CAP) is a regulatory protein involved in the transcription of several operons in Escherichia coli. cAMP-independent, nonspecific complexes of CRP and DNA were investigated by photochemical cro
Publikováno v:
Journal of Biological Chemistry. 266:23461-23466
Polyglutamylation, a new posttranslational modification of tubulin identified originally on the acidic alpha variants by Edde et al. (Edde, B., Rossier, J., Le Caer, J. P., Desbruyeres, E., Gros, F., and Denoulet, P. (1990) Science 247, 83-85), consi
Autor:
Philippe Denoulet, Yoheved Berwald-Netter, Annette Koulakoff, J.P. Le Caer, Bernard Eddé, Jérôme Rossier, François Gros
Publikováno v:
Journal of Cellular Biochemistry. 46:134-142
We describe the presence of alpha-tubulin and MAP2 acetyltransferase activities in mouse brain. The enzyme(s) copurified with microtubules through two cycles of assembly-disassembly. Incubation of microtubule proteins with [3H]acetyl CoA resulted in
Publikováno v:
Science. 247:83-85
The high degree of tubulin heterogeneity in neurons is controlled mainly at the posttranslational level. Several variants of alpha-tubulin can be posttranslationally labeled after incubation of cells with [3H]acetate or [3H]glutamate. Peptides carryi
Publikováno v:
Journal of protein chemistry. 16(5)
Axonemal tubulin exhibits a high degree of heterogeneity mostly due to several posttranslational modifications (PTM). The aim of this work was to chemically characterize the different PTM occurring in the C-terminal tail of axonemal tubulin purified
Autor:
J.P. Le Caer, Jérôme Rossier, André Adoutte, Jean-Marie Schmitter, Nicolette Levilliers, Marie-Hélène Bré, Virginie Redeker
Publikováno v:
Science (New York, N.Y.). 266(5191)
A posttranslational modification was detected in the carboxyl-terminal region of axonemal tubulin from Paramecium. Tubulin carboxyl-terminal peptides were isolated and analyzed by Edman degradation sequencing, mass spectrometry, and amino acid analys
Autor:
M. Dubarry, J.-P. Cartron, Patrick Lambin, S. Chrétien, P. Rouger, C. T. Craescu, J.P. Le Caer, Claude Lopez, A. Ben Ghanem, J. J. Winchenne, N. Casadevall
Publikováno v:
Preparative biochemistry. 24(2)
A recombinant human erythropoietin (rH-EPO) was obtained from the culture supernatants of human B-lymphoblastoid cells transfected by the human EPO gene. rH-EPO was purified by a two-step method based on immunoaffinity and ion exchange chromatography