The exotoxin P. aeruginosa: a proenzyme having an unusual mode of activation.
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Adenosine Diphosphate Sugars↗
Biomedical subjects
S H Leppla
Publications and source records attributed to S H Leppla.
Large-scale purification and characterization of the exotoxin of Pseudomonas aeruginosa.
The exotoxin (PE) of Pseudomonas aeruginosa was purified from 50-liter cultures by a simple three-step procedure, yielding 135 mg of essentially homogeneous protein. In Ouchterlony gel diffusion, PE produces a single line which does not interact with a diphtheria toxin-antitoxin precipitin line. The protein has a molecular weight of 66,000, an isoelectric point of 5.1, N-terminal arginine, and four disulfide bridges. The amino acid composition shows no apparent similarity to that of diphtheria toxin. The median lethal dose of this PE preparation in mice weighing 20 g is 0.1 mug. The median lethal dose in 350-g rats is 20 mug. The cytotoxicity of PE for mouse L929 fibroblasts is completely neutralized by small amounts of specific pony antitoxin. The exotoxin possesses adenosine diphosphate-ribosylation activity. Both cytotoxic and adenosine diphosphate-ribosylation activities are shown to be properties of the intact 66,000-dalton protein.
Adenosine Diphosphate↗
Comparison of the 3' termini of discrete segments of the double-stranded ribonucleic acid genomes of cytoplasmic polyhedrosis virus, wound tumor virus, and reovirus.
The 3' terminal nucleosides of the isolated components of double-stranded ribonucleic acids of reovirus, wound tumor virus, and cytoplasmic polyhedrosis virus were determined by labeling with tritiated sodium borohydride. All wound tumor virus and cytoplasmic polyhedrosis virus components appear to contain approximately equal amounts of U(OH) and C(OH) termini. Reovirus segments have essentially only C(OH) termini.
Adenosine↗
Characterization of the subunit structure of the ribonucleic acid genome of influenza virus.
Ribonucleic acid extracted from influenza virus was labeled at the 3' termini with (3)H and analyzed by polyacrylamide gel electrophoresis. Influenza virus was found to contain a minimum of seven and possibly as many as 10 polynucleotide chains, most of which appear to terminate at the 3' end in uridine.
Animals↗