Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Jeanne Feinberg"'
Publikováno v:
International Journal of Peptide and Protein Research. 47:62-69
Gelsolin and thymosin β4 appear to be two important actin-associated proteins involved in the regulation of actin polymerization. It has been widely demonstrated that thymosin is the major cellular actin-sequestering factor shifting the polymerizati
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:
Biochemical and Biophysical Research Communications. 233:61-65
The binding of the N-terminal domain (S1) of gelsolin to monomeric actin has been extensively documented. In contrast, the location of the C-terminal calcium dependent domains (S4-6) interacting with the actin filament during the severing process rem
Publikováno v:
Biopolymers. 41(6)
Gelsolin, a calcium and inositol phospholipid-sensitive protein, regulates actin filament length. Its activity is complex (capping, severing, etc.) and is supported by several functional domains. The N-terminal domain alone (S1), in particular, is ab
Publikováno v:
FEBS Letters. (2):237-240
Publikováno v:
European journal of biochemistry. 153(2)
Brevin, an actin-severing protein present in serum from numerous mammals, has been purified to homogeneity from bovine serum, using hydrophobic chromatography as the last purification step. The physicochemical parameters of brevin have been establish
Publikováno v:
European journal of biochemistry. 82(1)
Cyanogen bromide cleavage of yeast 3-phosphoglycerate kinase yielded four fragments which account for the amino acid composition of the entire molecule. These results are consistent with a single polypeptide chain of molecular weight 42 000. Affinity