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Ghafoorunissa

Publications and source records attributed to Ghafoorunissa.

25 records · Page 2Linked to original sources

Plasma amino acid pattern in pellagra.

Plasma free amino acid levels were determined in subjects suffering from pellagra and compared with levels observed in normal subjects of both low and high socioeconomic groups. In pellagrins, a wide variation was seen in the plasma levels of tryptophan and these levels overlapped considerably with those in the low socioeconomic group controls. Administration of 5 g L-leucine daily for 5 days to normal subjects belonging to the low socioeconomic group did not affect the plasma tryptophan levels. These data suggest that the pellagragenic action of leucine is not mediated through changes in circulating levels of tryptophan. They also indicate that a low level of plasma tryptophan per se may not be a reliable biochemical indicator in the diagnosis of pellagra.

Adult↗

Effect of dietary protein on the biosynthesis of inositol in rat testes.

The presence of inositol in high concentrations in semen and the male reporductive organs of mammals suggests that it may have an important rôle in male reproduction. The present study is an attempt to investigate the effect of dietary protein restriction in the male rat on inositol synthesis in the testes and on the concentration of inositol in some of the accessory sex organs. The results show that marginal protein deficiency does not alter either the biosynthesis of inositol or inositol concentration in the testis, epididymis or seminal vesicles.

Animals↗

Effect of leucine on enzymes of the tryptophan-niacin metabolic pathway in rat liver and kidney.

Dietary excess of leucine affects tryptophan-niacin metabolism adversely and has thus been implicated in the etiology of pellagra. To understand the biochemical basis of leucine-induced changes in tryptophan-niacin metabolism the effect of leucine on enzymes of tryptophan-niacin metabolism was investigated. Excess of leucine in the diet had no effect on rat liver 3-hydroxyanthranilate oxygenase and nicotinate phosphoribosyltransferase but significantly decreased the activity of quinolinate phosphoribosyltransferase of rat liver and kidney. The activities of tryptophan oxygenase in liver and picolinate carboxylase in kidney were significantly higher in leucine-fed animals than in the controls. Also, oxidation of [U-(14)C]tryptophan in vivo was higher in leucine-fed animals. Increased picolinate carboxylase and decreased quinolinate phosphoribosyltransferase activities would result in a decrease in NAD formation from dietary tryptophan. Lowered NAD formation from tryptophan particularly when the niacin concentrations in the diet are marginal would result in a state of conditioned niacin deficiency.

Journal Article↗