• N Jayanthi Bai

      Articles written in Journal of Biosciences

    • Alpha-tocopheryl acetate hydrolase in chicken liver. Characterisation and properties

      V N R Kartha N Jayanthi Bai Thomas George S Krishnamurthy

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      An enzyme catalysing the hydrolysis ofa-tocopheryl acetate was characterised in chicken liver. The enzyme was localised in the microsomes, had an optimum pH 8.6 and aKm value of 0.5 mM. The enzyme did not hydrolyse retinyl acetate, cholesteryl acetate and ethyl acetate, thus indicating a high degree of specificity.a-Tocopheryl acetate hydrolase required bile salts as a specific co-factor. The results suggested a role for this enzyme in the absorption of vitamin E.

    • Fructose diphosphate aldolase-class I (Schiff base) fromMycobacterium tuberculosis H37Rv

      N Jayanthi Bai M Ramachandra Pai P Suryanarayan Murthy T A Venkitasubramanian

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      An aldolase was partially purified from fermenter grownMycobacterium tuberculosis H37Rv cells. The aldolase has a molecular weight of 150,000, possesses a tetrameric structure and cleaves both fructose diphosphate and fructose-1-phosphate, the former being cleaved 17 times faster. The enzyme was inactivated by treatment with NaBH4 in the presence of fructose diphosphate or dihydroxyacetone, phosphate suggesting Schiff base formation during its catalytic function. Thiol reagents, EDTA and metal ions had no apparent effect on the aldolase activity. These results show that aldolase is of Class I type. However, this enzyme, unlike the mammalian Class I aldolase, was unaffected by carboxypeptidase A. N-ethylmaleiniide and dithionitrobenzoic acid.

    • Effect of retinol on the hemolysis and lipid peroxidation in vitamin E deficiency

      S Krishnamurthy Thomas George N Jayanthi Bai

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      A study on the effect of retinolin vitro on the hemolysis of vitamin E deficient rat red blood cells showed that retinol enhanced the lysis of the E deficient cells as compared to the lysis of normal cells. The lipid peroxidation present during hydrogen peroxide induced lysis of E deficient cells was however markedly inhibited in the presence of retinol without affecting the rate of lysis. In an actively peroxidising system of non-enzymatic lipid peroxidation of rat liver or brain homogenates and of brain lysosomes incubated with human erythrocytes, no lysis was obtained; incorporation of retinol in such systems resulted in lysis but no peroxidation. Hydrogen peroxide generating substances almost completely inhibited the lysis of normal human erythrocytes by retinol, but linoleic acid hydroperoxide and auto-oxidised liver or brain homogenates and ox-brain liposomes increased the lysis. It is concluded that vitamin E deficient erythrocyte hemolysis may be augmented by retinol, an anti-oxidant, having a lytic function without the peroxidation of stromal lipids

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