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1.
J Biosci ; 1989 Mar; 14(1): 55-61
Article in English | IMSEAR | ID: sea-160708

ABSTRACT

Chronic administration of ethanol in rats caused the reduction of serum cholesterol binding reserve. The very low density and high density lipoproteins, main serum cholesterol binding reserves, were slightly increased with corresponding increases in their lipid and protein components during initial stage of alcohol consumption. However, these capacities get deminished during reversal of hyperlipemia induced by prolonged action of ethanol. This situation may be an early indicator for the initiation of hepatic damage and a variety of secondary effects of ethanol.

2.
J Biosci ; 1988 Sep; 13(3): 269-274
Article in English | IMSEAR | ID: sea-160679

ABSTRACT

The levels of lipid peroxides in circulatory lipoproteins increased with chronic administration of ethanol or acetaldehyde. Low density lipoprotein showed a greater increase in its content of lipid peroxides than very low density lipoprotein or high density lipoprotein. However, very low density lipoprotein was more prone to lipid peroxidation in vitro than low density lipoprotein or high density lipoprotein. The effect of acetaldehyde was more marked than that of ethanol. Lipoproteins of control and hyperlipemic groups were partially protected against peroxidation by butyrated hydroxytoluene and serum high density lipoprotein of normal rats.

3.
J Biosci ; 1987 Mar; 12(1): 55-59
Article in English | IMSEAR | ID: sea-160561

ABSTRACT

The levels of lipoprotein-X in circulation increased with chronic administration of ethanol or acetaldehyde. A similar profile was seen in rat serum with alkaline phosphatase activity and bilirubin content. Total cholesterol, phospholipids and triglyceride contents increased followed by a decrease by progressive feeding with ethanol or acetaldehyde. The effect of acetaldehyde was more pronounced than that of ethanol.

4.
J Biosci ; 1981 Sept; 3(3): 311-320
Article in English | IMSEAR | ID: sea-160165

ABSTRACT

The interactions of flavin mononucleotide (riboflavin-5'-monophosphate) with two polypeptides, poly-(α-L-lysine) and poly-(α-L-histidine) in water and 0.05 Μ phosphate buffer were studied by measuring circular dichroism in the pH range 3 to 11. The interation of flavin mononucleotide with the two polypeptides was due to hydrophobic as well as ionic associations and was further influenced by the involvement of the ribityl side chain. The results of the present study have shown that small changes in the environmental conditions of the interacting molecules could modify their mode of interaction considerably.

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