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pro vyhledávání: '"D L, Cinti"'
Autor:
D L, Cinti
Publikováno v:
Connecticut medicine. 60(2)
The Combined M.D./Ph.D. Degree Program (CDP) of the University of Connecticut School of Medicine is an intensive seven-year program that allows exceptional students simultaneously to develop both clinical and research skills. Each year the program ac
Publikováno v:
The Journal of Cell Biology
Further evidence for organelle interaction during drug metabolism by the liver is presented. The apparent stimulation by succinate of formaldehyde accumulation in the medium, which was reported to occur with liver slices and homogenates as well as wi
Publikováno v:
Journal of Biological Chemistry. 251:1571-1577
The oxidation of formaldehyde by rat liver mitochondria in the presence of 50 mM phosphate was enhanced 2-fold by exogenous NAD+. Absolute requirement of NAD+ for formaldehyde oxidation was demonstrated by depleting the mitochondria of their NAD+ con
Publikováno v:
Journal of Biological Chemistry. 255:11357-11364
Publikováno v:
Journal of Biological Chemistry. 255:1867-1873
Publikováno v:
The Journal of biological chemistry. 258(24)
The present study provides strong evidence for the involvement of rat liver microsomal cytochrome b5 in the first reduction step of fatty acid chain elongation. The rate of reoxidation of NADH-reduced microsomal cytochrome b5 was markedly stimulated
Publikováno v:
The Journal of biological chemistry. 261(29)
The present study examines the effect of the acetylenic thioester dec-2-ynoyl-CoA (delta 2 10 identical to 1-CoA) on the microsomal fatty acid chain elongation pathway in rat liver. When the individual reactions of the elongation system were measured
Autor:
D. L. Cinti, Juris Ozols
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461590286
Incubation of rat cytochrome b5 (D-b5) with rat liver microsomes resulted in specific binding of the hemoprotein. The bound hemoprotein was rapidly reduced by NADH. The NADH cytochrome c reductase activity in these preparations increased in proportio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::360b1f736d5e11f0163bfc040c2b4368
https://doi.org/10.1007/978-1-4615-9026-2_32
https://doi.org/10.1007/978-1-4615-9026-2_32
Autor:
D L, Cinti, J, Ozols
Publikováno v:
Advances in experimental medicine and biology. 58(00)
Incubation of rat cytochrome b5 (D-b5) with rat liver microsomes resulted in specific binding of the hemoprotein. The bound hemoprotein was rapidly reduced by NADH. The NADH cytochrome c reductase activity in these preparations increased in proportio
Autor:
D L, Cinti, M R, Montgomery
Publikováno v:
Molecular pharmacology. 13(1)