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K T Shetty

Publications and source records attributed to K T Shetty.

34 records · Page 2Linked to original sources
PubMed1990

Phosphoserine phosphatase of human brain: partial purification, characterization, regional distribution, and effect of certain modulators including psychoactive drugs.

Phosphoserine phosphatase (PSPase), a cytosolic enzyme has been purified 106 fold from human brain, by employing conventional protein purification techniques. The use of MgCl2 (10 mM) and chloroform treatment, during purification enabled the removal of non-specific proteins. The final enzyme preparation exhibited a broad pH optimum of 5.6-6.6 and could dephosphorylate both L and D enantiomers of the phosphoserine, but with different Km values for O-P-L serine (3.6 x 10(-5) M) and O-P-D serine (1 x 10(-4) M). Enzyme activity was found to be specific for phosphoserine, whereas other phosphoesters including phosphothreonine and phosphoproteins such as casein and phosvitin were found to be poor substrates. The enzyme activity was uncompetitively inhibited by L-serine. Further the PSPase activity was inhibited by vanadate, (41%), trifluoperazine (23%), chlorpromazine (34%) at an equimolar concentration of 1 mM, whereas lithium and ethanol did not influence the enzyme activity. Minor tranquilizers such as diazepam and chlordiazepoxide activated the enzyme activity to an extent of 13% and 59% respectively. In addition, species and regionwise heterogeneity was observed with respect to distribution of enzyme activity in six major areas of human, rabbit and rat brains.

Animals↗
PubMed1981

Occurrence of gamma-glutamyl transpeptidase activity in several mycobacteria including Mycobacterium leprae.

gamma-Glutamyl transpeptidase (gamma-GT) activity, which catalyzes the transfer of the "gamma-glutamyl" group of gamma-glutamyl compounds to several dipeptide and amino acid acceptors, was found to be present in several mycobacteria, including M. leprae, both in cell suspensions and in cell-free sonicates. Glycyl D-amino acids were active as acceptors, particularly glycyl-D-alanine and alpha, epsilon-diaminopimelic acid, among the amino acids. Two mycobacterial isolates obtained from biopsy material of lepromatous patients also exhibited similar enzyme activity. The need for further work to delineate the possible role of gamma-GT in mycobacterial metabolism is strongly indicated.

Animals↗
PubMedDate not supplied

Type Ib glycogenosis.

Type Ib glycogenosis is a rare glycogen storage disorder resulting from a defect in the enzyme, glucose-6-phosphatase microsomal translocase. We report a case of Type Ib glycogenosis in an 18 month-old male child who presented with a history of hypoglycemic seizures and recurrent infections and had a massive hepatomegaly, recurrent hypoglycemia, hyperuricemia, hypertriglyceridemia, neutropenia and fasting lactacidemia which decreased sharply on glucose administration.

Glycogen Storage Disease Type I↗
PubMedDate not supplied

Arginase deficiency.

Hyperargininemia due to arginase deficiency is a rare, inherited, urea cycle disorder. We report a case of arginase deficiency in a 5-year old boy presenting with mild hyperammonemia, hyperargininemia, and dibasic aminoaciduria.

Child, Preschool↗
PubMedDate not supplied

GM2 gangliosidoses: a review of cases confirmed by beta-N-acetylhexosaminidase assay.

The inborn errors of GM2 ganglioside metabolism cause GM2 ganglioside to accumulate within the lysosomes of the nerve cells. The majority of the patients are infants with the Tay-Sachs form of the disease associated with a severe deficiency of beta-N-Acetylhexosaminidase A (hexosaminidase A). Both Hexosaminidase A and B are deficient in Sandhoff disease. The serum total hexosaminidase and the percentage of hexosaminidase A and B were estimated in 449 patients who presented with progressive mental-motor retardation. Three cases of Tay-Sachs disease and two cases of Sandhoff disease were detected. They presented with exaggerated startle response to acoustic stimuli, seizures, optic atrophy and retinal cherry red spots in addition to psychomotor retardation. One case of Sandhoff disease had hepatosplenomegaly and skeletal deformities.

Child, Preschool↗
PubMedDate not supplied

Methodological aspects of aldehyde dehydrogenase assay by spectrophotometric technique.

Aldehyde dehydrogenase (ALDH) activity was assayed spectrophotometrically by measuring the increase in delta A at 340 nm, as a criteria of NAD conversion to NADH in the presence of propionaldehyde. The effect of pH and substrate(s) concentration of nonenzymatic increase in absorbance at 340 nm was studied. Results indicate that the increase in absorbance at 340 nm is not entirely due to NAD conversion to NADH. It was observed that nonenzymatic interaction of NAD and aldehyde could as well result in increase in absorbance at 340 nm. The magnitude of the nonenzymatic contribution towards increase in absorbance at 340 nm is found to be pH, substrate(s) conc., and time dependent. Further, the observed nonenzymatic reaction product was found to be different from that of NADH as confirmed by u.v. spectral characteristics (lambda max. 346 nm) and its inability to activate NADH/NADPH-dependent glutathione reductase. Based on these findings, a final assay method comprising a substrate blank consisting of NAD and aldehyde, and the assay pH of 7.4 is recommended for measuring the ALDH activity. Further, under these experimental conditions the Km value of human RBC ALDH was found to be 0.59 mM for propionaldehyde substrate.

Aldehyde Dehydrogenase↗
PubMedDate not supplied

Diazepam- and chlordiazepoxide-mediated increases in erythrocyte aldehyde dehydrogenase activity and its possible implications.

Erythrocyte ALDH activity was assayed in alcoholic (n = 70) and nonalcoholic (n = 40) subjects. In general, alcoholics without any prior medications (n = 57) were found to have a decreased ALDH activity (mean +/- SD: 3.38 +/- 1.7 mU; p less than 0.001) as compared to control group (5.10 +/- 1.57 mU). However, a group of alcoholics who were detoxified with benzodiazepines (n = 13) prior to blood collection for enzyme assay were found to have higher ALDH activity (4.92 +/- 2.46 mU; p less than 0.05) as compared to alcoholics who were not detoxified. In vitro experiments demonstrated that both diazepam (DZM) and chlordiazepoxide (CDP) could activate the ALDH. The magnitude of enzyme activation by DZM and CDP appear to correlate with their relative potency of tranquilizing effect. Further, the observed ability of DZM to reverse the inhibition of ALDH mediated by disulfiram may explain the biochemical basis of the reported ability of benzodiazepines (BDZ) to reduce the intensity of disulfiram ethanol reaction (DER).

Adult↗
PubMedDate not supplied

Effect of disulfiram administration on rat brain glutathione metabolism.

Chronic administration of disulfiram (DS) to rats was found to affect glutathione (GSH) metabolism. Glutathione was measured in the rat brain following DS administration. Reduced glutathione was decreased significantly (1.52 +/- 0.3 mumol/g; p < 0.001), with a concomitant increase in oxidised glutathione (GSSG) content (0.12 +/- 0.013 mumol/g; p < 0.001) in the brain as a consequence of DS treatment. However, total glutathione (GSH + GSSG) content of the experimental group did not show any appreciable change. Similar changes were observed in the liver following chronic DS treatment. Brain glutathione reductase (GR) activity was found to be significantly depleted (100 +/- 0.16 mumol/min/mg protein), but glutathione peroxidase (GP) activity was not affected in rats chronically treated with DS. It is reported that the treatment with DS decreases the GSH content, with a concomitant increase in GSSG level, and perturbs the GSH/GSSG redox status, inducing an oxidative stress on the brain. Glutathione reductase implicated in maintaining GSH/GSSG homeostasis by replenishing GSH is also affected by DS potentiating the oxidative damage of the tissue. This effect of DS on glutathione metabolism in the brain would explain some of its known neurotoxic effects.

Animals↗