par Reyns, Claude 
;Leonis, José ;Schlusselberg, Jean
Référence Biochimie, 57, 2, page (123-129)
Publication Publié, 1975-05
;Leonis, José ;Schlusselberg, Jean Référence Biochimie, 57, 2, page (123-129)
Publication Publié, 1975-05
Article révisé par les pairs
| Résumé : | Fumarase from chicken heart is purified 400 times from the crude muscle extract. The isolation procedure includes ammonium sulfate fractionations, Bio-Gel P-300 column chromatography and electrofocusings on pH-gradients from pH 3 to 10 and from pH 7 to 9. Chicken fumarase behaves as an homogeneous protein in sedimentation, diffusion and electrofocusing studies ; the protein possesses a single amino-terminal residue : lysine. The analysis of the CD and ORD spectra suggests the presence of 60-65 p. cent of α-helix, 0 - 5 p. cent of β-structure with the remaining portions of the protein in an unordered conformation. Chicken fumarase is found to be composed of 4 subunits of identical molecular weight (51.000) and devoid of disulfide bridges. Finally, the physicochemical properties of chicken fumarase are compared with those of the porcine enzyme. © 1975. |
