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Journal ArticleDOI

Effects of vitamin E deficiency on the activities of lipid-requiring enzymes in rabbit liver and muscle.

TLDR
In vitamin E-deficient rabbits, the specific activities at 37 degrees of mitochondrial oligomycin-sensitive ATPase, beta-hydroxybutyrate dehydrogenase, NADH cytochrome C reductase and Ca-ATPase, and microsomal glucose-6-phosphatase were increased and reduced, reflecting changes in the microenvironment of membrane-bound enzymes as a consequence of vitamin E depletion.
Abstract
The effects of vitamin E deficiency on membrane integrity were studied by examining the temperature dependence of membrane-bound enzyme activities in liver mitochondria and microsome and in muscle sarcoplasmic reticulum. In vitamin E-deficient rabbits, the specific activities at 37 degrees of mitochondrial oligomycin-sensitive ATPase (EC 3.6.1.3), beta-hydroxybutyrate dehydrogenase (EC 1.1.1.30), and microsomal glucose-6-phosphatase (EC 3.1.3.9) were increased, whereas those of microsomal NADH cytochrome C reductase (EC 1.6.99.3) and sarcoplasmic reticulum Ca-ATPase were reduced in comparison to control rabbits. Arrhenius plots of activity against temperature yielded a linear plot over the range 10 to 40 degrees in the case of beta-hydroxybutyrate dehydrogenase, NADH cytochrome C reductase and Ca-ATPase, and multiple discontinuities for glucose-6-phosphatase and oligomycin-sensitive ATPase. In control rabbits, all five enzymes showed a single discontinuity in the Arrhenius plot over the range 16 to 19 degrees. These results reflect changes in the microenvironment of membrane-bound enzymes as a consequence of vitamin E depletion.

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Journal ArticleDOI

Vitamin E and selenium participation in fatty acid desaturation. A proposal for an enzymatic function of these nutrients.

TL;DR: It is proposed that vitamin E and selenium play a role in the desaturation of n-3 and n-6 polyunsaturated fatty acids by participating in the microsomal electron transport chain and in a proposed peroxidase moiety of the desaturase complex, respectively.
Journal ArticleDOI

Fluorescence depolarization studies of phase transition and fluidity in lecithin liposomes containing alpha-tocopherol.

TL;DR: The results suggest that the effect of alpha-tocopherol in lowering the phase-transition temperature depends on its hydrophobic side chain, and that its effect in decreasing the membrane fluidity above thephase-transitions temperature depends in part on its hydrophylic chroman ring portion.
Journal ArticleDOI

Vitamin E deficiency and the susceptibility to lipid peroxidation of mouse cardiac and skeletal muscles.

TL;DR: The results show that a short-term vitamin E deficiency affects the peroxidative properties of cardiac and skeletal muscles and may thus expose the muscles to peroxidation injuries.
Journal ArticleDOI

Effects of Vitamin E Deficiency on the Distribution of Cholesterol in Plasma Lipoproteins and the Activity of Cholesterol 7α-Hydroxylase in Rabbit Liver

TL;DR: Results suggested that accumulation of cholesterol observed in dystrophic muscle of vitamin E-deficient rabbits may be due to an increase in LDL and VLDL cholesterol, the plasma lipoproteins carrying cholesterol to peripheral tissue, and to a decrease in cholesterol 7 alpha-hydroxylase activity, whose activity may have been affected by the reduced level of cytochrome P-450.
References
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Journal Article

Protein Measurement with the Folin Phenol Reagent

TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Journal ArticleDOI

Effects of Phospholipid Acyl Chain Fluidity, Phase Transitions, and Cholesterol on (Na+ + K+)-stimulated Adenosine Triphosphatase

TL;DR: Cholesterol, which is known to reduce the fluidity of phospholipid fatty acyl chains, inhibits phosphoipid-stimulated (Na + K)-ATPase activity, and the inhibition is complete, however, only with saturatedospholipids.
Journal ArticleDOI

The influence of membranes on the temperature-induced changes in the kinetics of some respiratory enzymes of mitochondria.

TL;DR: The results suggest that the temperature-induced change in activation energy of the membrane-bound enzymes is associated with a phase change in the lipid component of the membranes which induces a configurationalchange in the enzyme proteins.
Journal ArticleDOI

Regulation of Microsomal Enzymes by Phospholipids II. ACTIVATION OF HEPATIC URIDINE DIPHOSPHATE-GLUCURONYLTRANSFERASE

TL;DR: The activation of UDP-glucuronyltransferase in these experiments cannot be attributed to compartmentation of the enzyme but is due to phospholipid-induced alterations of enzyme conformation.
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