Two arginyl-transfer ribonucleic acid (tRNA) synthetase (EC 6.1.1.13, arginine: ribonucleic acid ligase adenosine monophosphate) activities were found in extracts of Escherichia coli strains AB1132 and NP2. The two arginyl-tRNA synthetase activities in extracts of strain AB1132 were found to be separable by diethylaminoethyl-cellulose column chromatography, Sephadex column fractionation, and by...

The extracellular Opacity Factor elaborated by a strain of group A streptococcus M type 2 was purified by ammonium sulphate precipitation, DEAE-cellulose and hydroxylapatite column chromatography and Sephadex G-200 gel filtration. Gel filtration experiments indicated that the Opacity Factor is consituted of high molecular weight proteins or protein aggregates which appear to dissociate into sub...

Synchronous plasmodia of Physarum polycephalum were pulse-labeled with 3H-thymidine in early or late portions of the S-phase, and the binding capacity of the replicated DNA for isochronous S-phase plasmodial proteins assessed by nitrocellulose filter binding assay. Replication units replicating during the first one-third of the S-phase preferentially bind cytosol proteins present in plasmodia e...

A Streptococcus sanguis 133-79 adhesin identified by the monoclonal antibody 1.1 (MAb 1.1) binds both saliva-coated hydroxylapatite (sHA) and platelets. The complementary binding site(s) for the adhesin was identified by the anti-idiotypical MAb 2.1. To learn if this adhesion system, marked by the antiadhesin MAb 1.1 and anti-binding site MAb 2.1, is commonly used by strains within the sanguis ...

DNA synthesized by particulate fractions from human leukemic white blood cells has been subfractionated by hybridization to Rauscher leukemia virus 70S RNA followed by hydroxylapatite chromatography. The Rauscher-leukemia-virus-specific DNA fraction is shown to be complementary only to sequences present in the nuclear DNA of Balb/c mouse spleens infected by this virus and the nuclear DNA from h...

An enzyme catalyzing the reduction of S-(2,4-dichlorophenacyl)glutathione to 2',4'-dichloroacetophenone was purified to apparent homogeneity by ion exchange, gel filtration, and hydroxylapatite chromatography from rat hepatic cytosol. The molecular weight was 30,000-37,000. The enzyme is distinct from the glutathione S-transferases, mercaptopyruvate sulfurtransferase, and glyoxalase I. Substrat...

Epoxide hydrase was solubilized from liver microsomes of phenobarbital-treated rats by treatment with cholate and purified to apparent homogeneity by ammonium sulfate fractionation and column chromatography in the presence of the nonionic detergent Emulgen 911 on DEAE-cellulose and hydroxylapatite. The purified enzyme preparation had a single major band with a molecular weight of 53,000 to 54,0...