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R S Ranu

Publications and source records attributed to R S Ranu.

41 records · Page 3Linked to original sources
PubMed1972

Evidence for specific inhibition of translocation of aminoacyl-transfer ribonucleic acid by the pretreatment of ribosomes of Bacillus subtilis with p-chloromercuribenzoate.

The biological activities of Bacillus subtilis ribosomes pretreated with 0.5, 1, or 2 mmp-chloromercuribenzoate (PCMB) were examined. The ribosomes treated with 1 or 2 mm PCMB lost their capacity to synthesize polyphenylalanine as well as the capacity to bind phenylalanyl-transfer ribonucleic acid. On the other hand, approximately 70% of the polyphenylalanine synthesis capacity was lost with ribosomes pretreated with 0.5 mm PCMB. This inhibition was found to be due to a specific inhibition of the translocation step. The effect of 0.5 mm PCMB was reversed by 20 mm Mg(2+) without the loss of PCMB bound to ribosomes, while beta-mercaptoethanol partially reversed the inhibitory effect with concomitant loss of bound PCMB.

Bacillus subtilis↗
PubMed1971

Effect of sulfhydryl reagents on the ribosomes of Bacillus subtilis.

The effect of various sulfhydryl reagents on the ribosomes of Bacillus subtilis was studied. The 70S ribosomes were completely dissociated into 30S and 50S subunits by appropriate concentrations of p-chloromercuribenzoic acid (PCMB) and 5,5'-dithio-bis-(2-nitro-benzoic acid). The N-ethylmaleimide and iodoacetamide failed to dissociate the ribosomes even at relatively high concentrations. The rate of dissociation of ribosomes by PCMB varied with the concentration of ribosomes. A progressive decrease in the rate of dissociation was observed as the concentration of ribosomes in the reaction mixture was increased. The PCMB-induced ribosomal subunits were unable to reassociate into 70S monomers unless they were dialyzed against buffer containing beta-mercaptoethanol. On the average, four molecules of PCMB per 70S ribosome and two molecules of PCMB per each 30S and 50S subunit were bound. The number of PCMB molecules bound per ribosome did not change with increasing concentrations of PCMB, even though higher concentrations of PCMB resulted in dissociation of ribosomes into subunits.

Bacillus subtilis↗
PubMed1968

Serological activity of protein A of Staphylococcus aureus: the precipitinogen as an antigen for determining antibodies by the passive hemagglutination test.

Tanned sheep erythrocytes have been considered incapable of sensitization with the precipitinogen of protein A of Staphylococcus aureus, so that the activity of this antigen in serological reactions has so far been studied by means of the agar diffusion test (ADT) only. The precipitinogen of the protein A in this study was found to become attached to the tanned erythrocytes and to sensitize them for the passive hemagglutination test (PHT). It was determined that, in contrast to nonspecific reactivity between normal human serum and the precipitinogen in the ADT, the reaction in the PHT was of specific nature. Of seven species studied, all normal human, dog, and hog sera tested were positive in the PHT. However, the hemagglutinin titers of the sera of the two animal species by far exceeded those of the human sera. The data emphasized the usefulness of the highly sensitive PHT for assaying antibodies to protein A.

Animals↗