Zobrazeno 1 - 10
of 64
pro vyhledávání: '"Louise Anne Pradel"'
Autor:
Jeanne Feinberg, Dalila Karoui, Hervé Rochat, Claude Roustan, Jana Gregoire, Louise-Anne Pradel, Abdellatif Fattoum
Publikováno v:
International Journal of Peptide and Protein Research. 17:393-400
The purpose of this work was to contribute to the study of the covalent struc ture of yeast 3-phosphoglycerate kinase. First, we undertook the complete align ment of the four fragments produced by cyanogen-bromide cleavage and which constitute the in
Publikováno v:
Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, 2001, 1510 (1-2), pp.18-28. ⟨10.1016/s0005-2736(00)00262-5⟩
Biochimica et Biophysica Acta:Biomembranes, 2001, 1510 (1-2), pp.18-28. ⟨10.1016/s0005-2736(00)00262-5⟩
International audience; Annexin 2 is a member of the annexin family which has been implicated in calcium-regulated exocytosis. This contention is largely based on Ca(2+)-dependent binding of the protein to anionic phospholipids. However, annexin 2 wa
Autor:
Fran¸oise Regnouf, Bruno Delouche, Ginette Devilliers, Isabelle Sagot, Louise-Anne Pradel, Jean-Pierre Henry, Jean Cartaud
Publikováno v:
Journal of Biological Chemistry. 270:27143-27150
Heterotetrameric annexin 2 phosphorylated "in vitro" by rat brain protein kinase C is purified and obtained devoid of unphosphorylated protein; it contains 2 mol of phosphate/mol of heterotetramer. The aggregative and binding properties of the phosph
Publikováno v:
European Journal of Biochemistry. 205:85-91
Tryptic digestion of brain spectrin generates a number of fragments from alpha and beta subunits; when these fragments are incubated with F-actin or neurofilament light subunit, four of them with molecular masses below 30 kDa sediment with the cytosk
Publikováno v:
Biology of the Cell. 75:45-54
Annexins I and 2 are Ca2+-binding proteins related to the cytoskeletal proteins which have been reported to bind in a calcium-dependent manner to F-actin and phospholipidsin vitro. Proteins immunologically related to the brain 37-kDa annexin I and 36
Publikováno v:
Journal of neurochemistry. 68(4)
Annexin 2 phosphorylated in vitro by protein kinase C has been shown to restore partially catecholamine secretion in streptolysin O-permeabilized chromaffin cells depleted of their protein kinase C activity. This result suggested a phosphorylation of
Autor:
Louise-Anne Pradel, A. Rendon
Publikováno v:
FEBS letters. 327(1)
Previously we have purified annexin 1 [J. Neurochem. 56 (1991) 1985-1986] from pig cerebral cortex as a monomeric protein of 37 kDa. Here, the localization of annexin 1 was investigated in subcellular fractionations of rat cerebral cortex using immun
Publikováno v:
Journal of neurochemistry. 56(6)
Five proteins having molecular masses of 90, 67, 37, 36, and 32 kDa (p90, p67, p37, p36, and p32, respectively) were identified in the particulate fractions of pig brain cortex and pig spinal cord prepared in the presence of 0.2 mM Ca2+ and further p
Publikováno v:
European Journal of Biochemistry; Mar75 Part 2, Vol. 52 Issue 2, p345-350, 6p
Publikováno v:
European Journal of Biochemistry. 122:153-161
Plasma membranes of thyroid cells were purified from hog thyroid glands following two procedures. Their homogeneity was tested by electron microscopy and by measurements of the activity of membrane-bound enzyme markers. According to the procedure use