PubMed Health⌕ Search

Biomedical subjects

M Maiti

Publications and source records attributed to M Maiti.

At least 55 records · Page 3Linked to original sources

Structural polypeptides of cholera bacteriophage phi 2.

The structural polypeptides of the cholera bacteriophage phi 2 have been analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Eight different polypeptides were identified. The apparent molecular weights of the polypeptides were 143 000, 96 500, 68 000, 53 000, 37 500, 29 500, 21 000, and 13 500, respectively. The percentage of total protein corresponding to each polypeptide was estimated.

Bacteriophages↗

Polyacrylamide gel electrophoresis and infrared spectroscopy of vibrio biotypes.

Polyacrylamide gel electrophoresis and infrared spectroscopy were used to study the relationship between Vibrio cholerae (classical), Vibrio cholerae (El Tor), and nonagglutinable (NAG) vibrios. Acid extracts of the different strains produced type-specific electrophoretic patterns, and the infrared spectra revealed broad absorption maxima which largely correspond to those found in other organisms. With the exception of the NAG vibrios, the infrared spectra of cholera El Tor vibrios were identical. Strain-specific differences were found in the exoprotein spectra of these organisms by the sodium dodecyl sulphate - polyacrylamide gel electrophoretic technique.

Bacterial Proteins↗

Mode of action of bacteriophage phi 149 on cholera and El Tor vibrios.

Bacteriophage phi 149 which was propagated in Vibrio cholerae (classical) OGAWA 154 strain, killed Vibrio cholerae (El Tor) strain MAK 757 without phage propagation. El Tor vibrios underwent a small degree of lysis only when infected by the phage phi 149 at a high multiplicity of infection and lost their viability at a rate-dependent multiplicity of phage infection. Evidence was obtained with 32P-labelled bacteriophage phi 149 for penetration of phage DNA into both bacterial strains. In host strain (OGAWA 154) phage particle synthesis occurred normally. In El Tor strain MAK 757 the phage DNA was not degraded but its expression was blocked. The killing effect of phi 149 on El Tor strain MAK 757 is supposed to be due to damage of the cytoplasmic membrane, which could not be repaired under the influence of phage information. This was indicated by a blockage of cellular respiration and RNA and protein synthesis.

Bacterial Proteins↗

Interaction of furazolidone with DNA.

DN forms a complex with furazolidone producing thereby a quenching and a bathochromic shift of the drug absorption pattern. The binding isotherm was a non-linear one indicating involvement of more than one binding process in the formation of the furazolidone - DNA complex. The furazolidone - DNA complex inhibited digestion of DNA by DNAase and stabilized DNA against thermal strand separation by a significant degree.

Binding Sites↗

Effects of furazolidone on the infection of Vibrio cholerae by bacteriophage phi149.

Furazolidone in concentrations which had little effect on the growth of host organisms greatly reduced the yield of phage phi149 from the host Vibrio cholerae OGAWA 154. This phage was resistant to the in vitro action of the drug. The phage yield of infected bacteria depended significantly on the time of addition or withdrawal of the drug. The average burst size of the drug-treated and infected bacteria decreased exponentially with increase in drug concentration. The latent period of phage multiplication and also the eclipse period did not change significantly from the control values. A concentration of 0.05 mug of furazolidone per ml inhibited DNA synthesis by about 50% in phage-infected cells and only by about 18% in noninfected ones, relative to the respective controls. RNA and protein synthesis were affected by a much smaller degree both in infected and noninfected cells. Quantitative deduction of the length of furazolidone-treated cells from their phage adsorption characteristics and its agreement with previous electron microscopy data indicated that furazolidone did not affect the phage receptors.

Adsorption↗