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K Sengupta

Publications and source records attributed to K Sengupta.

48 records · Page 3Linked to original sources
PubMed1981

Relationship among isoproterenol, cyclic AMP, cyclic AMP-dependent protein kinase and lipolysis in perfused fat cells.

By using perfused fat cells the effect of isoproterenol on adenosine 3':5'-monophosphate (cAMP) levels, cAMP-dependent protein kinase activity and lipolysis was studied. An infusion of isoproterenol (10(-7) M) resulted in a time-dependent increase in cAMP levels and protein kinase activity in the fat cells. Both parameters reached maximum values after 5 min of drug infusion, then declined to steady-state values by 10 min. At 60 min, cAMP levels were still significantly (P less than .05) elevated over basal. Dose-response curves were determined for isoproterenol on cAMP levels, protein kinase activity and glycerol release. All three parameters were increased by isoproterenol over the same concentration range (10(-9)--10(-7) M). A plot of cAMP levels or protein kinase activity ratios vs. glycerol release resulted in linear relationship with high degrees of correlation (r = 0.98). The rates at which cAMP levels and glycerol release decline after termination of isoproterenol infusion were studied. Half-life values of 5.8 and 6.9 min were obtained for cAMP levels and glycerol release, respectively. These results support the hypotheses that cAMP, acting through protein kinase, is an intracellular mediator of the lipolytic response to isoproterenol. It is concluded that cAMP is not formed in great excess of that necessary to maximally increase lipolysis.

Adipose Tissue↗
PubMed1980

Regulation of formation in vivo of pyridoxal phosphate in hydrazine-treated rats.

The formation in vivo of pyridoxal phosphate was studied in hydrazine-treated rats. hydrazine was administered i.p. at a dose of 1.28 mg/day (20% LD50) for each 100 g body weight for 7 days. Hydrazine administered at the present dose did not appear to have an effect on the pyridoxal phosphate level of either liver on kidney tissue. Hydrazine treatment, however, elevated the pyridoxal level in liver, while kidney pyridoxal level remained unaltered under the same condition. The pyridoxine phosphate oxidase activity in liver, unlike that in kidney, was found to be increased after hydrazine treatment. The increase in pyridoxine phosphate oxidase activity in the liver of hydrazine-treated rats was prevented by actinomycin D treatment. It has been suggested that hydrazine treatment at the present dose enhanced the rate of formation of pyridoxal phosphate from pyridoxine-5-phosphate in liver, while the formation of pyridoxal phosphate in kidney appeared to be independent of hydrazine treatment. The increased activity of liver pyridoxine phosphate oxidase in hydrazine-treated rats was ascribed to the induction of the enzyme. It has been further suggested that the unalteration in the liver pyridoxal phosphate level in hydrazine-treated rats inspite of enhanced conversion of pyridoxine-5-phosphate to pyridoxal phosphate, was probably caused by the increased hydrolysis of pyridoxal phosphate.

Animals↗
PubMed1978

Induction of dominant lethals with ethyl methane-sulfonate in male germ cells of mulberry silkwork, Bombyx mori l.

Sensitivity of male germ cells in the mulberry silkworm, Bombyx mori L., to ethyl methanesulfonate (EMS) was determined by treating newly emerged 5th- instar larvae, and 2-day- and 7-day-old pupae with 3 concentrations, 0.05, 0.1 and 0.15%, of the mutagen. The frequency of dominant-lethal mutations induced by EMS treatment was used as the parameter for the study. Spermatids and spermatozoa were markedly sensitive to EMS. Statistical analysis confirmed that differences in respect of percentage of egg hatch among the 3 different treatments as well as the interactions between the 3 factors, e.g. stages, hatchability and EMS treatment, were highly significant.

Animals↗
PubMed1978

Some studies on ascorbic acid metabolism in hydrazine-treated rats.

The metabolism of ascorbic acid was studied in hydrazine-treated rats. Hydrazine was administered i.p. at a dose of 1.28 mg/day (20% LD50) for each 100 g body weight for 7 days. Hydrazine administration at the present dose did not appear to have an effect on the total ascorbic acid level of liver, kidney, spleen and testis. The adrenal and plasma total ascorbic acid levels were, however, elevated. The activity of liver D-glucuronoreductase and that of liver and kidney dehydroascorbatases were diminished after hydrazine administration. The changes in the activities of liver enzymes were accompanied by a fall in the reduced ascorbic acid level and an elevation in the dehydroascorbic acid level. The uronolactonase activity of liver, on the other hand, remained independent of hydrazine treatment. It has been suggested that hydrazine treatment at the present dose reduced the biosynthesis of L-ascorbic acid from D-glucuronolactone as substrate. In spite of diminished synthesis, the normal level of total ascorbic acid in the liver of hydrazine-treated rats was maintained by reducing the degradation of L-ascorbic acid. The rise in the plasma total ascorbic acid level after hydrazine treatment was ascribed to reduced catabolism and urinary excretion of ascorbic acid, while the elevation in adrenal total ascorbic acid level might result from increased uptake of ascorbic acid by the gland from blood or from nonfunctional accumulation.

Alcohol Oxidoreductases↗
PubMed1976

Effects of L-lysine administration on certain aspects of ascorbic acid metabolism.

The effects of administration of L-lysine on total ascorbic acid level of various tissues and plasma of rats were studied. The biosynthesis of L-ascorbic acid by the liver tissue was also followed. L-lysine was administered at a dose of 88.3 mg day-1 (20% of LD50) for each 100 g body weight for 14 days. L-lysine administration at the present dose elevated the total ascorbic acid level of liver, kidney, testes, spleen and brain tissues. The plasma total ascorbic acid level was also elevated. The synthesis of L-ascorbic acid from both D-glucuronolactone and L-gulonolactone by the liver was, however, reduced after L-lysine administration. It has been suggested that L-lysine administration at the present dose altered the plasma amino acid pattern which in turn impaired the in vivo synthesis of tissue proteins and, consequently, the synthesis of apoproteins of ascorbic acid-synthesizing enzymes, the D-glucuronoreductase and L-gulonooxidase, were reduced. The elevation in the total ascorbic acid level of extra-hepatic tissues and plasma after L-lysine administration was ascribed to the reduced catabolism and diminished urinary excretion of ascorbic acid.

Animals↗
PubMedDate not supplied

Production and characterization of monoclonal antibodies against a highly immunogenic fraction of Entamoeba histolytica (NIH:200) and their application in the detection of current amoebic infection.

Six monoclonal antibodies (MAbs) were produced against a highly immunogenic fraction derived by the chromatographic separation of the soluble preparation of axenic Entamoeba histolytica (strain NIH:200) trophozoites. Isotype characterization of the six MAbs revealed that four belonged to the IgM class and one each to the IgG1 and the IgG2a subclasses. The immunoreactivity patterns and the specificity of the MAbs with homologous and heterologous antigens were analyzed by the enzyme-linked immunotransfer blot technique and by the enzyme-linked immunosorbent assay. The MAbs reacted intensely with isolates of E. histolytica (strain NIH:200 as well as a local isolate MX1) but showed no reactivity with Entamoeba coli, Iodamoeba butschlii, Endolimax nana, Entamoeba hartmanni, free-living amoeba (Acanthamoeba harticolus) and other enteric parasites. Using the IgG1 MAb as a detecting antibody, a polyclonal-monoclonal antibody-based enzyme-linked immunosorbent assay was developed for the detection of E. histolytica antigens in stool samples of infected patients. The detection limit of the assay was 8 ng of amoebic antigen. This test was found to be specific and sensitive and yielded 100% positive results in cases with amoebiasis but did not react with controls included in the evaluation. The MAb-based enzyme-linked immunosorbent assay developed in this study will be an important test for the diagnosis of E. histolytica in the feces of infected humans; however, the limitation of the test is the inability to discriminate the pathogenic status of the amoeba detected in the stool.

Animals↗