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A O Summers

Publications and source records attributed to A O Summers.

60 records · Page 4Linked to original sources
PubMed1977

Plasmid-determined resistance to tellurium compounds.

Transferable plasmids in gram-negative bacteria that confer resistance to potassium tellurite or tellurate were found. This re-istance was distinct from resistance to mercury, silver, or arsenic compounds and was unrelated to antibiotic resistance. In Escherichia coli, plasmids determine a 100-fold increase in the minimal inhibitory concentration for tellurite and a 10-fold increase in tellurate resistance. Many, but not all, of the plasmids belong to incompatibility group S. In Pseudomonas aeruginosa, tellurium resistance is specifically associated with incompatibility group P-2 and involves a 5- to 10-fold increase in tellurite or tellurate resistance.

Anti-Bacterial Agents↗
PubMed1977

Outer membrane proteins of Escherichia coli. V. Evidence that protein 1 and bacteriophage-directed protein 2 are different polypeptides.

Protein 1 from the outer membrane of Escherichia coli K-12 and protein 2 from a phage PA-2 lysogen of the same strain were isolated by differential sodium dodecyl sulfate extraction and purified by ion-exchange and gel filtration chromatography. Rabbit antisera were prepared against these proteins and showed no cross-reaction between proteins 1 and 2. The proteins have the same N-terminal amino acid but show small yet significant differences in amino acid composition. The proteins were cleaved with cyanogenbromide in solvents containing both formic acid and trifluoroacetic acid. By comparing the cleavage in these solvents, it was established that protein 1 yielded 5 cyanogen bromide peptides, and the sum of the molecular weights of these was equivalent to the molecular weight of the uncleaved protein. Protein 2 yielded 4 cyanogen bromide peptides, none of which was identical to those of protein 1, and the sum of these peptides was also equivalent to the apparent molecular weight of the uncleaved protein. Significant differences were also observed when tryptic peptides from the two proteins were compared. These results indicate that protein 1 and the phage-directed protein 2 are distinct, different, and apparently homogeneous proteins.

Amino Acids↗
PubMed1974

Cell-free mercury(II)-reducing activity in a plasmid-bearing strain of Escherichia coli.

The ability to reduce Hg(II) to Hg(0), which is determined by a plasmid-borne gene in Escherichia coli, is conferred by a Hg(II)-inducible activity which is located in the cytoplasm rather than in the periplasmic space of the cell. This Hg(II)-reducing activity can be isolated from the supernatant of a 160,000 x g centrifugation after French Press disruption of the cells. The activity is dependent on glucose-6-phosphate, glucose-6-phosphate dehydrogenase, and 2-mercaptoethanol, but is not enhanced by added nicotinamide adenine dinucleotide phosphate. Treatment of the active fraction with N-ethylmaleimide causes irreversible loss of the Hg(II)-reducing activity. Unlike the Hg(II)-reducing activity found in intact cells, the cell-free activity is not inhibited by toluene, potassium cyanide, or m-chlorocarbonylcyanide-phenylhydrazone; however, it is inhibited by Ag(I) and phenylmercuric acetate to the same extent as the activity in intact cells. Neither phenylmercuric acetate nor methylmercuric chloride is reduced to Hg(0) by the cell-free activity. Au(III), however, is a substrate for the cell-free activity; it is reduced to metallic colloidal Au(0).

Alkaline Phosphatase↗
PubMed1972

Mercury resistance in a plasmid-bearing strain of Escherichia coli.

A strain of Escherichia coli carrying genes determining mercury resistance on a naturally occurring resistance transfer factor (RTF) converts 95% of 10(-5)m Hg(2+) (chloride) to metallic mercury at a rate of 4 to 5 nmoles of Hg(2+) per min per 10(8) cells. The metallic mercury is rapidly eliminated from the culture medium as mercury vapor. The volatilizing activity has a temperature dependence and heat sensitivity characteristic of enzymatic catalysis and is inducible by mercuric chloride. Ag(+) and Au(3+) are markedly inhibitory of mercury volatilization.

Catalysis↗
PubMed1968

Production of highly labeled adenoviruses.

A method is described for increasing the incorporation of radioactive thymidine into adenovirus deoxyribonucleic acid by the use of amethopterin. In addition, a modified procedure is presented for the preparation of highly purified adenoviruses. This procedure, which employs enzymatic digestion of cellular debris, obviates the necessity for fluorocarbon treatment of crude virus suspensions, and routinely provides excellent recovery of virus.

Adenoviridae↗