Measurement of Cytochrome Kinetics in Rat Liver Mitochondria by Stopped Flow and Dual-Wavelength Spectrophotometry

1979 ◽  
pp. 77-81
Author(s):  
Angelo Azzi ◽  
Hubert Affolter
Keyword(s):  
Rat Liver ◽  
Liver Mitochondria ◽  
Dual Wavelength ◽  
Rat Liver Mitochondria ◽  
Stopped Flow

Dual coenzyme activities of high-Km aldehyde dehydrogenase from rat liver mitochondria

1990 ◽  
Vol 68 (4) ◽  
pp. 751-757 ◽  
Author(s):  
C. Stan Tsai ◽  
D. J. Senior
Keyword(s):  
Steady State ◽  
Rat Liver ◽  
Aldehyde Dehydrogenase ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Binary Complex ◽  
Stopped Flow ◽  
Conformation Change ◽  
Rate Limiting ◽  
Flow Burst

Various kinetic approaches were carried out to investigate kinetic attributes for the dual coenzyme activities of mitochondrial aldehyde dehydrogenase from rat liver. The enzyme catalyses NAD+- and NADP+-dependent oxidations of ethanal by an ordered bi-bi mechanism with NAD(P)+ as the first reactant bound and NAD(P)H as the last product released. The two coenzymes presumably interact with the kinetically identical site. NAD+ forms the dynamic binary complex with the enzyme, while the enzyme-NAD(P)H complex formation is associated with conformation change(s). A stopped-flow burst of NAD(P)H formation, followed by a slower steady-state turnover, suggests that either the deacylation or the release of NAD(P)H is rate limiting. Although NADP+ is reduced by a faster burst rate, NAD+ is slightly favored as the coenzyme by virtue of its marginally faster turnover rate.Key words: aldehyde dehydrogenase, coenzyme preference.

Effects of 5-5'-Diphenyl-2-thiohydantoin (DPTH) and Thyroxine on the Ultrastructure and Chemical Composition of Rat Liver

1971 ◽  
Vol 29 ◽  
pp. 570-571
Author(s):  
E. A. Elfont ◽  
R. B. Tobin ◽  
D. G. Colton ◽  
M. A. Mehlman
Keyword(s):  
Chemical Composition ◽  
Rat Liver ◽  
Future Study ◽  
Mode Of Action ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Effective Inhibitor ◽  
Biochemical Effects ◽  
Glycerophosphate Dehydrogenase ◽  
Stimulation Of

Summary5,-5'-diphenyl-2-thiohydantoin (DPTH) is an effective inhibitor of thyroxine (T4) stimulation of α-glycerophosphate dehydrogenase in rat liver mitochondria. Because this finding indicated a possible tool for future study of the mode of action of thyroxine, the ultrastructural and biochemical effects of DPTH and/or thyroxine on rat liver mere investigated.Rats were fed either standard or DPTH (0.06%) diet for 30 days before T4 (250 ug/kg/day) was injected. Injection of T4 occurred daily for 10 days prior to sacrifice. After removal of the liver and kidneys, part of the tissue was frozen at -50°C for later biocheailcal analyses, while the rest was prefixed in buffered 3.5X glutaraldehyde (390 mOs) and post-fixed in buffered 1Z OsO4 (376 mOs). Tissues were embedded in Araldlte 502 and the sections examined in a Zeiss EM 9S.Hepatocytes from hyperthyroid rats (Fig. 2) demonstrated enlarged and more numerous mitochondria than those of controls (Fig. 1). Glycogen was almost totally absent from the cytoplasm of the T4-treated rats.

Energy and Antioxidant Status of Rat Liver Mitochondria during Hypoxia- Reoxygenation of Different Duration

2016 ◽  
Vol 7 (4) ◽  
pp. 349-361
Author(s):  
Olga A. Gonchar ◽  
Valentina I. Nosar ◽  
Larisa. V. Bratus ◽  
I. N. Tymchenko ◽  
N. N. Steshenko ◽  
...  
Keyword(s):  
Rat Liver ◽  
Antioxidant Status ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Hypoxia Reoxygenation
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