Vallabhaneni V. Rao

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A soluble enzyme that catalyzes the oxidation of L-alpha-aminoadipate delta-semialdehyde to L-alpha-aminoadipic acid in the presence of NAD+ has been isolated and characterized from human liver. This enzyme L-alpha-aminoadipic delta-semialdehyde oxidoreductase has been found to be localized in the cytosol using subcellular fractionation and marker enzyme(More)
By using a sensitive radioactive assay method, we present here evidence that L-pipecolic acid oxidase is localized in both mitochondria and peroxisomes of rat liver. Brain white matter contained a more than 2-fold higher activity of L-pipecolic acid oxidation than the brain cortex. Suborganellar fractionation studies indicate that while the enzyme is a(More)
1. Developmental aspects of L-lysine-ketoglutarate reductase, the first enzyme in saccharopine pathway of L-lysine degradation in rat liver and brain tissues were studied. 2. Although the adult rat brain shows negligible activity, the enzyme activity was shown to be highly active during the early stages of development. 3. The enzyme activity gradually(More)
Intracerebral administration of L-alpha-aminoadipic acid (L-AAA) at 500 mg/kg body weight to rats caused a complex behavioral change with sporadic wet-dog shakes. Animals developed severe limbic seizures between 1 and 6 h after L-AAA injection, characterized by generalized convulsions. Twenty days after L-AAA injection kynurenine aminotransferase (KAT)(More)
L-Pipecolate oxidase, an enzyme that oxidizes L-pipecolic acid in the human liver has been demonstrated in the peroxisomal preparation. This enzyme oxidizes L-pipecolic acid with concomitant production of H2O2 in the peroxisome of the normal human liver. The immediate product of L-pipecolic acid oxidation has been identified as L-alpha-aminoadipate(More)
A direct assay method is described for L-pipecolate oxidase. The assay uses NaHSO3 to trap the L-alpha-amino [3H]adipate delta-semialdehyde (AAS) formed as a direct reaction product of L-pipecolate oxidase from L-[3H]pipecolic acid. The adduct so formed was separated from the substrate on Dowex 50 (H+) column. The product was identified as [3H]AAS by amino(More)
Overexpression of P-glycoprotein, the plasma membrane protein prod uct of the MURI gene, is a major determinant in the development of resistance to a large number of cancer chemotherapeutic agents. A battery of antibodies, including the MURI gene-specific monoclonal antibody mi.\ln C494, is used to evaluate human tissues in clinical multidrug resistance(More)
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