Zobrazeno 1 - 6
of 6
pro vyhledávání: '"C A CaJacob"'
Autor:
E, Valdivia, C, Gabel, J E, Reardon, C A, CaJacob, H, Yang, R S, Wehbi, G L, Scott, P A, Frey, L A, Fahien
Publikováno v:
Scanning microscopy. 6(3)
This study reports morphological and functional alterations observed in respiring isolated mitochondria when they are exposed to nonpenetrating, positive electrostatically charged synthetic undecagold clusters. Modification of the undecagold clusters
Autor:
David E. Williams, P. R. Ortiz De Montellano, Bettie Sue Siler Masters, C A CaJacob, A. S. Muerhoff, N O Reich
Publikováno v:
Journal of Biological Chemistry. 264:749-756
Terminal acetylenic fatty acid mechanism-based inhibitors (Ortiz de Montellano, P. R., and Reich, N. O. (1984) J. Biol. Chem. 259, 4136-4141) were used as probes in determining the substrate specificity of rabbit lung cytochrome P-450 isozymes of pre
Publikováno v:
Journal of Biological Chemistry. 260:14610-14615
When the pyruvate dehydrogenase complex of Escherichia coli is reduced by NADH and alkylated by N-[14C]ethylmaleimide, 19-20 nmol of N-[14C]ethylmaleimide are bound per mg of complex. This is in accord with the presence of 10 nmol of functional lipoy
Publikováno v:
The Journal of biological chemistry. 263(35)
Cytochrome P-450LA omega purified from clofibrate-induced rat liver oxidizes lauric acid to 11- and 12-hydroxydodecanoic acid in approximately a 1:17 ratio at a rate of 20 nmol/nmol P-450/min. In contrast, cytochrome P-450b oxidizes lauric acid much
Publikováno v:
The Journal of biological chemistry. 260(27)
When the pyruvate dehydrogenase complex of Escherichia coli is reduced by NADH and alkylated by N-[14C]ethylmaleimide, 19-20 nmol of N-[14C]ethylmaleimide are bound per mg of complex. This is in accord with the presence of 10 nmol of functional lipoy
Autor:
A S, Muerhoff, D E, Williams, N O, Reich, C A, CaJacob, P R, Ortiz de Montellano, B S, Masters
Publikováno v:
The Journal of biological chemistry. 264(2)
Terminal acetylenic fatty acid mechanism-based inhibitors (Ortiz de Montellano, P. R., and Reich, N. O. (1984) J. Biol. Chem. 259, 4136-4141) were used as probes in determining the substrate specificity of rabbit lung cytochrome P-450 isozymes of pre