Search PubMed⌕ Search

Biomedical subjects

R K Ghosh

Publications and source records attributed to R K Ghosh.

At least 37 records · Page 2Linked to original sources
PubMed1988

Characterization of the phage-specific transfer RNA molecules coded by cholera phage phi 149.

Aminoacylation of tRNA isolated from choleraphage phi 149-infected cells with individual 3H-labeled L-amino acids followed by hybridization with phage DNA revealed that the phage encodes tRNAs specific for arginine, proline, glycine, isoleucine, serine, valine, tyrosine, histidine, lysine, leucine, tryptophan, and aspartic acid. Aminoacylation of phage-coded tRNAs isolated from phage DNA-RNA hybrids also confirmed this observation except for tryptophan.

Bacteriophages↗
PubMed1988

Characterization of phage-specific transfer RNA molecules coded by Vibrio eltor phage e4.

Transfer RNAs were isolated from phage e4-infected Vibrio eltor Mak 757 cells. These were aminoacylated with 14 individual 3H-labeled L-amino acids. Hybridization of these [3H]aminoacyl-tRNAs with phage e4 DNA revealed that the phage e4 encodes tRNAs for arginine, tryptophan, tyrosine, leucine, and isoleucine. Direct aminoacylation of phage-coded tRNA molecules isolated from phage DNA-RNA hybrids also confirmed this observation.

Bacteriophages↗
PubMed1988

Toxin profiles of Vibrio cholerae non-O1 from environmental sources in Calcutta, India.

A collection of Vibrio cholerae non-O1 isolated from the aquatic environs of Calcutta, a cholera-hyperendemic area, were examined for the production of cholera toxin (CT), Shiga-like toxins (Vero toxins), heat-stable enterotoxin, and hemolysins. Two (0.5%) V. cholerae non-O1 isolates produced CT. The DNA from both these isolates also hybridized with a DNA probe containing sequences encoding the A subunit of CT. None of the strains produced Shiga-like toxins or heat-stable enterotoxin. Hemolytic activity was observed in 89.7% of the strains, of which 36.1% exhibited biological activity in the suckling mouse. However, none of them produced a hemolysin that cross-reacted with the thermostable direct hemolysin of Vibrio parahaemolyticus. It appears from this study that a small percentage of environmental V. cholerae non-O1 strains do possess the potential for causing cholera-like diarrhea.

Cholera↗
PubMed1987

Characterization of Vibrio eltor typing phages: properties of the Eltor phage e4.

Biophysical characteristics of Vibrio eltor phage e4, a key phage in the Vibrio cholerae typing scheme were studied. This icosahedral phage was found to contain 12 structural polypeptides with mol. wt. ranging from 25,000 to 120,000. One of these polypeptides of mol. wt. 50,000 accounted for most of the structural proteins present and was probably the major phage capsid protein. The phage genome comprised a single linear, double-stranded DNA molecule, 69.2 kbp in length (45.6 X 10(6) mol. wt.) as determined by electron microscopy and restriction fragment analyses. The G + C content was 34.6%. Electron microscopy data indicated that unlike the DNAs of other cholera phages, phage e4 DNA is not circularly permuted. Adsorption under normal conditions was biphasic with rate constants of 1.02 X 10(-9)/ml/min up to 60% adsorption and 3 X 10(-10)/ml/min thereafter. Intracellular phage multiplication was characterized by a latent period of 27 min. The burst size was approximately 100 phage particles per infected cell.

Adsorption↗
PubMed1987

Induction of hepatic mitochondrial alpha-glycerophosphate dehydrogenase by L-triiodothyronine in Singi fish (Heteropneustes fossilis Bloch).

A single injection of L-triiodothyronine (T3) in different doses (0.25, 0.5, 5, 20 and 50 micrograms/g) increased the hepatic mitochondrial cytochrome-linked alpha-glycerophosphate dehydrogenase (alpha-GPD) activity and mitochondrial protein content of Singi fish, as observed on the 3rd day. A non-linear dose-response relationship with respect to enzyme activity was observed with different doses of T3. A low dose of 0.1 micrograms of T3 per g failed to cause any change in alpha-GPD activity and mitochondrial protein content of the liver. The enhancement of alpha-GPD activity over the control level with a low and a high dose of T3, viz., 0.5 and 5 micrograms/g, was followed from the 1st to the 7th day, when it was found that enzyme activity reached the maximum level on the 3rd day and then gradually declined to the control value on the 7th day. The percentage increase in enzyme activity with 5 micrograms/g was higher than that with 0.5 microgram/g from the 2nd to 5th day. Compared to the control, these two doses of T3 caused an increase in alpha-GPD activity from the 1st to the 6th day. Cycloheximide inhibited the T3-induced increase in alpha-GPD activity, mitochondrial and total protein content of liver. Immersion of Singi fishes in thiourea-containing (1 mg/ml) medium for 30 days showed a fall in hepatic alpha-GPD activity in comparison to the euthyroid control. A single injection of T3 (0.5 microgram/g) to the hypothyroid fish recovered alpha-GPD activity to more than the euthyroid control level. An increase in mitochondrial protein content in the T3-injected hypothyroid fish has been observed. DNA content of the fish liver remained unchanged in every experimental condition. The results thus showed the significant responsiveness of the fish liver to thyroid hormone.

Animals↗
PubMed1986

Metabolic reactions responsible for glucose stimulation of alkaline phosphatase in Vibrio cholerae.

Alkaline phosphatase activity in Vibrio cholerae strain 569B grown in low-phosphate medium was stimulated if glucose or glycerol was used as the carbon source. No such stimulation was observed, however, if tricarboxylic acid cycle intermediates like succinate or citrate were used. Experiments using specific enzyme inhibitors strongly indicated that the metabolic reactions of the glycolytic pathway from glyceraldehyde 3-phosphate to 2-phosphoglycerate play a key role in the stimulation process.

Alkaline Phosphatase↗
PubMed1985

Evidence that a system similar to the recA system of Escherichia coli exists in Vibrio cholerae.

Two lines of evidence suggest that a gene analogous to the recA gene of Escherichia coli exists in Vibrio cholerae and that its product serves a proteolytic function in the SOS response. Firstly, Southern blot hybridization using the recA gene of E. coli as a probe revealed a genomic sequence in V. cholerae which hybridized with the probe. Secondly, the SOS-like response in V. cholerae (as measured by beta phage induction) triggered by DNA damaging agents like Furazolidone could be blocked by Antipain, a protease inhibitor known to inhibit RecA protease action in E. coli. Maximal blocking effect of Antipain on beta phage induction occurred at 1 mM. At this concentration neither the viability of the host bacterium nor the lytic growth of a clear plaque mutant of the phage was affected by Antipain.

Antipain↗
PubMed1983

Synthesis of phage-specific transfer RNA molecules by vibriophage phi 149.

32P-Labelled tRNA was isolated from uninfected and phage phi 149-infected Vibrio cholerae cells. These tRNA preparations were then hybridised with DNA isolated from phage phi 149. Significant hybridisation was observed only with tRNA from phage phi 149-infected cells. This strongly suggests that infection of classical vibrio with phage phi 149 results in the synthesis of phage-specific tRNA molecules.

Bacteriophages↗
PubMed1982

Repression of the alkaline phosphatase of Vibrio cholerae.

The synthesis of alkaline phosphatase by two strains of Vibrio cholerae belonging to the Inaba and Ogawa serotypes has been examined in relation to the phosphate concentration of the culture medium. The synthesis of the enzyme in both strains was repressed in cells grown in the presence of a high concentration of inorganic phosphate. Lowering the phosphate content of the growth medium led to a derepression of enzyme activity. The presence of glucose in low phosphate medium stimulated the degree of derepression. The synthesis of the enzyme by strain Inaba 569B was more sensitive to inorganic phosphate than that of strain Ogawa 154. The enzyme was presumably located in the periplasmic space since it was released when the organisms were converted to spheroplasts.

Alkaline Phosphatase↗
PubMed1982

Monomeric alkaline phosphatase of Vibrio cholerae.

Alkaline phosphatase has been purified to homogeneity from two strains of Vibrio cholerae. The enzymes from both strains are single polypeptides of molecular weight 60,000. Both of the enzymes have pH optima around 8.0 and can act on a variety of organic phosphate esters, glucose-1-phosphate being the best substrate. The enzymes are unable to hydrolyze ATP and AMP. Although they have identical Km values, the two enzymes differ significantly in Vmax with p-nitrophenyl phosphate as substrate. The enzymes from the two strains also differ in their sensitivity to EDTA, Pi, and metal ions and activities of the apoenzymes. Ca2+ reactivated the apoenzymes most.

Alkaline Phosphatase↗
PubMed1982

Effect of thyroxine on protein and nucleic acid contents of different parts of brain of Singi fish (Heteropneustes fossilis Bloch).

Effects of three consecutive days injections of thyroxine (T4) of different doses (1, 2 and 4 micrograms/g of body weight) on different parts of the brain of Singi fish were studied. T4 enhanced the cranio-somatic index and the weight of different substructures of brain, viz., cerebrum, cerebellum midbrain and medulla oblongata, of Singi fish at 25 degrees C. Compared to the control, the protein content of cerebrum increased with all doses of T4 (1, 2 and 4 micrograms/g) and the RNA content of this region increased only with higher doses (2 and 4 micrograms/g). Cerebellum appeared to be relatively less responsive than cerebrum; T4 at the dose of 4 micrograms/g was only effective in increasing the protein content of the cerebellum, although the RNA content of this region was enhanced with both 2 and 4 micrograms of T4 per g. In midbrain and medulla oblongata, the protein content was elevated only with higher doses (2 and 4 micrograms/g) and RNA content was enhanced with all doses of T4 used. T4 injections did not cause any alteration of the DNA content of cerebrum and cerebellum, but in midbrain this cellular constituent increased in amount with all doses of T4 and in medulla oblongata it was increased with the dose of 2 or 4 micrograms of T4 per g body weight.

Animals↗
PubMed1980

Anatomical studies on the pudendal nerve in the Indian buffalo (Bubalus bubalis).

This is a study of the origin, formation, course and distribution of the pudendal nerve (N. pudendus) in the Indian buffalo (Bubalus bubalis). The pudendal nerve originates from the union of the ventral rami of the 2nd, 3rd and 4th sacral spinal nerves. The largest contribution comes from the 3rd sacral nerve (13,284 +/- 844.45 fibres). The number of fasciculi, their area and arrangement, the total fibre count and the diameter spectra of the myelinated nerve fibres in N. pudendus and its rami have also been studied. There are as many as 7-98 fascicles at different levels of this nerve. The mean value of the area of the fascicles ranges from 0.244-4.684 mm2. The histograms of the myelinated nerve fibres are unimodal at all the selected levels with a peak around 2-4 micrometer. Of the myelinated fibres 72.47-86.72% are in the range of 2-4 micrometer.

Animals↗
PubMed1978

Identification of an Escherichia coli nuclease acting on structurally altered transfer RNA molecules.

A nuclease (RNase D) that can recognize structurally altered transfer RNA molecules has been partially purified from Escherichia coli. The enzyme acts poorly on intact tRNA and is inactive with the synthetic polyribonucleotides, poly(A), poly(U), or double-stranded poly(A).poly(U). The enzyme requires Mg2+ for activity and is stimulated by the monovalent cations, K+ and NH4+. The products of the reaction are 5'-mononucleotides. The molecular weight of the protein is about 60,000 as judged by Sephadex G-100 chromatography. The enzyme does not correspond to any known E. coli ribonuclease and may represent an intracellular scavenging mechanism for denatured tRNAs and other inactive RNA molecules.

Cations↗
PubMed1978

Preparation of synthetic tRNA precursors with tRNA nucleotidyltransferase.

Rabbit liver tRNA nucleotidyltransferase can be used to substitute nucleotides within the -C-C-A sequence of tRNA or to add nucleotides following this sequence. These anomolous reactions of the enzyme have been used to prepare radioactively-labeled synthetic tRNA precursors which mimic the structure of the natural precursors. Under appropriate conditions synthetic precursors of defined structure can be made. In this paper we describe the synthesis of tRNA-C-[14C]U and tRNA-C-C-A-[14C]C-C, which are representative of tRNA precursors containing altered residues within the -C-C-A sequence or with extra residues following the normal 3'terminus. A variety of other possible precursors can also be prepared. These synthetic tRNA precursors have already proved useful for isolation of possible tRNA processing nucleases.

Animals↗
PubMed1978

Purification of potential 3' processing nucleases using synthetic tRNA precursors.

The synthetic tRNA precursors, tRNA-C-114C]U and tRNA-C-C-A-[14C]C-C, as well as poly (a) and diesterase-treated tRNA, have been used to identify and purify potential 3'processing nucleases. Four activities have been separated by this analysis; and three of them have been characterized. Two of the enzymes, which are well-separated on hydroxylapatite columns, act on poly(A), require K+ and Mg2+ for activity, and have molecular weights of about 90,000. These activities have properties previously ascribed to RNase II. The third enzyme does not act on poly(A), requires Mg2+ for activity, and has a molecular weight of about 60,000. It is identical to RNase D, previously characterized as an exonuclease acting on tRNAs with altered structure. Each of the enzymes can remove nucleotides from the tRNA precursor containing extra nucleotides beyond the 3'terminus, whereas they are relatively inactive with intact tRNA or tRNA-C-U. The greatest specificity was displayed by RNase D. The possibility that RNase D is a 3'processing nuclease is discussed.

Base Sequence↗