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Biomedical subjects

D S Pradhan

Publications and source records attributed to D S Pradhan.

At least 37 records · Page 2Linked to original sources
PubMed1984

Identification of a heat-labile cellular nuclease in Staphylococcus aureus with properties similar to the extracellular nuclease (EC 3.1.4.7).

Besides the well-known heat-stable extracellular staphylococcal nuclease (EC 3.1.4.7) and cell surface bound nuclease, one more nuclease, which is heat-labile, has been identified and purified on phosphorylated cellulose column and characterized. Analyses by Sephadex G-75 gel chromatography indicates that the heat-labile cellular nuclease has molecular weight of about 16,000 similar to those of extracellular and cell-surface bound nucleases. Like the heat-stable nucleases, the heat-labile enzyme acts on both DNA and RNA, is more active on heat-denatured DNA, requires Ca2+ ions for activity and maximum catalytic activity is observed at pH 9.8-10 and at 45 degrees C. The results suggest that the three enzymes have properties strikingly similar to one another and therefore may be related structurally.

Electrophoresis, Polyacrylamide Gel↗
PubMed1983

Uncoupling of oxidative phosphorylation in rat liver mitochondria following the administration of dimethyl sulphoxide.

A single intraperitoneal injection of 275 mg of dimethyl sulphoxide (DMSO) to rats (100-125 g body weight) effectively uncouples oxidative phosphorylation in liver mitochondria during the period from 2 hr to 5 day post-injection. Higher doses of DMSO are inhibitory to mitochondrial respiration. DMSO has however no uncoupling action on oxidative phosphorylation in vitro. On the other hand, dimethyl sulphide (DMS), a known metabolite of DMSO, brings about the uncoupling effect in vitro. The uncoupling of oxidative phosphorylation by normal mitochondria could also be achieved if these are pre-incubated (30 min at 0 degrees C) with the post-mitochondrial liver supernatant derived from rat injected with DMSO, 2-24 hr prior to sacrifice. These results provide explanation for the observed uncoupling effect exerted by DMSO in vivo.

Animals↗
PubMed1981

Reverse and forward reactions of carbamyl phosphokinase from Streptococcus faecalis R. Participation of nucleotides and reaction mechanisms.

The participation of Mg complex of nucleoside diphosphates and nucleoside triphosphates in the reverse and forward reactions catalyzed by purified carbamyl phosphokinase (ATP : carbamate phosphotransferase, EC 2.7.2.2) of Streptococcus faecalis R, ATCC-8043 were studied. The results of initial velocity studies of approx. 1 mM free Mg2+ concentration have indicated that in the reverse reaction MgdADP was as effective a substrate as MgADP. The phosphoryl group transfer from carbamyl phosphate to MgGDP, MgCDP and MgUDP was also observed at relatively higher concentrations of the enzyme and respective magnesium nucleoside diphosphate. In the forward direction MgdATP was found to be as efficient a phosphate donor as MgATP. On the other hand, Mg complexes of GTP, CTP and UTP were ineffective even at higher concentrations of the enzyme and respective magnesium nucleoside triphosphate. Product inhibition studies carried out at non-inhibitory level of approx. 1 mM free Mg2+ concentration have revealed that the enzyme has two distinct sites, one for nucleoside diphosphate or nucleoside triphosphate and the other for carbamyl phosphate or carbamate, and its reaction with the substrates is of the random type. Further tests of numerical values for kinetic constants have indicated that they are partially consistent with the Haldane relationship which is characteristic of rapid equilibrium and random mechanism.

Adenosine Diphosphate↗
PubMed1981

Extreme chemical mutagen sensitivity of respiratory adaptation in yeast.

The respiratory adaptation process (i.e. essentially mitochondrial biogenesis) in the cells of both wild-type Saccharomyces cerevisiae and strains sensitive to ultraviolet radiation (UV) undergoing transition from the anaerobic to the aerobic state (1-2 h aeration) could be arrested by a prior incubation for 15--30 min with several chemical mutagens and other DNA-acting chemicals at very low concentrations (10-7 to 10-6 M added to cells suspended at the density of 10(7) cells/ml). At the same concentrations, these chemicals also inhibited DNA and RNA biosynthesis in maturing mitochondria during respiratory adaptation. This provides suggestive evidence for the view that the inhibitory effect of the chemical mutagens on respiratory adaptation could be due to lesions introduced into the DNA of promitochondria in the anaerobic cells. The system of respiratory adaptation in S. cerevisiae cells could serve as a rapid test for ascertaining the potentiality of a chemical to affect cellular DNA and probably, in turn, its potentiality to be mutagenic.

Adaptation, Physiological↗
PubMed1979

Nature of RNAs synthesised in rat liver in response to hydrocortisone.

Experiments on hybridization of [32P]HnRNA from hydrocortisone-treated rat liver with rat-liver DNA, in competition with unlabelled liver HnRNA from hormone-deficient and treated rats, revealed marked differences in their nucleotide sequence homologies. It was found that the hormone-induced new species of HnRNAs were transcribed both on middle-repetitive and non-repetitive sequences of DNA. However similar differences in the sequence homologies were not detectable in respect of mRNA derived from livers of hydrocortisone-administered and adrenalectomised rats. The results imply that the new species of HnRNA synthesized following hormone treatment may be confined to the nucleus.

Adrenalectomy↗
PubMed1979

Liver RNA biosynthesis in adrenalectomized rats: effect of whole-body X-irradiation.

Exposure of rats to a single whole-body dose of X-rays led to an enhanced rate of RNA synthesis in the liver during 4 to 18 hours post-irradiation. This increase in RNA synthesis could not be obliterated by protecting the liver during irradiation. On the other hand, if adrenals were surgically removed prior to whole-body radiation exposure, no elevation either in liver RNA synthesis in vivo or liver chromatin template activity in vitro was apparent. Protection of only the head during irradiation could also prevent the stimulation in liver RNA synthesis in vivo. These results are suggestive of the involvement of neuro-endocrine reactions along the hypothalamus-pituitary-adrenal axes to be the underlying factors in whole-body radiation-evoked activation of the transcription machinery in the liver.

Adrenal Glands↗
PubMed1978

Syntheses of DNA and chromosomal proteins in the rat thymus following whole-body X-irradiation.

Syntheses of chromosomal proteins was studied in relation to DNA syntheses in the rat thymus following whole-body X-irradiation (600 rad). There was a considerable depression of the syntheses of DNA and histones during the first 4--48 hours after irradiation. The syntheses of histones H3 and H4 plus H2A were affected to a much greater degree than those of histones H1 and H2B, suggesting a tight coupling between the syntheses of DNA and histones H3 and H4 plus H2A. A part of the lysine-rich histones H1 and H2B, however, seems to be synthesized, even in the absence of DNA synthesis. Biosynthesis of non-histone proteins was also depressed in the thymus after irradiation. The degree of inhibition, however, was very low, except for the syntheses of a few non-histone protein components which were depressed to a considerable extent. This implies that the synthesis of the majority of non-histone proteins is independent of DNA synthesis.

Animals↗
PubMed1977

Induction of alkaline phosphatase in Escherichia coli. Effect of phenethyl alcohol.

Induction of alkaline phosphatase, an enzyme located in the periplasmic region of Escherichia coli, was inhibited by phenethyl alcohol, an agent believed to alter the cell membrane structure. Studies to elucidate mechanism of this inhibition showed that while phenethyl alcohol arrested the incorporation of [3H]leucine into active alkaline phosphatase, it did allow substantial incorporation of the label into inactive monomer subunits of the enzyme. These results suggest that phenethyl alcohol may not interfere with the de novo synthesis of monomer subunits of the enzyme but arrest conversion of these into active dimer enzyme presumably by its primary action on the cell membrane structure.

Alkaline Phosphatase↗
PubMed1977

Induction of alkaline phosphatase in Escherichia coli: effect of procaine hydrochloride.

The effect of procaine hydrochloride, an anesthetic known to alter membrane structure, on the induced formation of alkaline phosphatase, a periplasmic enzyme, in Escherichia coli was investigated. Procaine hydrochloride specifically arrested the appearance of active alkaline phosphatase while permitting the induction of another enzyme, beta-galactosidase, which is internally localized. Evidence has been obtained to show that procaine hydrochloride does not arrest synthesis of inactive monomer subunits of the enzyme, indicating that the drug interferes in the conversion of monomer subunits to an active dimer enzyme.

Alkaline Phosphatase↗