Palmer Rogers
University of Minnesota
32 Papers
272 Citations
Palmer Rogers is an academic researcher from University of Minnesota. The author has contributed to research in topics: Canavanine & Escherichia coli. The author has an hindex of 16, co-authored 32 publications.
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Papers
Differentiation of pathogenic and saprophytic leptospires with 8-azaguanine
Russell C. Johnson,Palmer Rogers +1 more
TL;DR: Growth of strains of the saprophyte Leptospira biflexa was almost insensitive to the bacteriostatic action of 8-azaguanine at concentrations varying from 25 to 600 mug/ml; these sa Prophytic leptospires were serially transferred five times in media containing 225 mug without any change in growth rate or cell yield.
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5-fluorouracil as a selective agent for growth of leptospirae.
Russell C. Johnson,Palmer Rogers +1 more
TL;DR: The use of 5-fluorouracil (FU) as a selective agent for the growth of leptospirae was investigated and canicola was successfully isolated from contaminated urine of experimentally infected dogs by use of the FU medium.
126
Studies in management of the contaminated wound: I. Technique of closure of such wounds together with a note on a reproducible experimental model
TL;DR: The increased likelihood of infection attending primary closure of contaminated wounds with percutaneous sutures gives strong support to the thesis that per cutaneous suture should be avoided in the closure of contaminated wounds.
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Clostridium acetobutylicum Mutants That Produce Butyraldehyde and Altered Quantities of Solvents
Palmer Rogers,Neil Palosaari +1 more
TL;DR: In this paper, allyl alcohol resistant mutants of Clostridium acetobutylicum NRRL B643 were selected and characterized, and the results supported the view that the type 2 AA mutants somehow alter normal regulated expression of the solvent pathway in C.acetobutyricum.
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Mechanism of canavanine death in Escherichia coli: II. Membrane-bound canavanyl-protein and nuclear disruption
TL;DR: The results suggest that the lethal action of l -canavanine involves incorporation of this analog into membrane-bound protein(s) that interrupts the normal organization and functioning of the E. coli genome.
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