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G M Levis

Publications and source records attributed to G M Levis.

30 records · Page 2Linked to original sources

R-mediated beta-lactamases and episomal resistance to the beta-lactam drugs in different bacterial hosts.

Ten penicillinase plasmids of varying taxonomic origin were studied after transfer to a variety of bacterial hosts. Nine of the ten plasmids specified enzymes with the following identical, or very similar, properties: substrate profile, molecular weight, susceptibility to heat and inhibitors, and electrophoretic mobility, i.e., TEM-like enzymes. The tenth R-mediated beta-lactamase was a cephalosporinase. Plasmids with TEM-like enzymes mediated resistance patterns identical towards the beta-lactam drugs, whereas the resistance pattern of the cephalosporinase plasmid was distinctly different. Expression of enzyme and resistance had a dual R-factor and host specificity. Escherichia coli K-12 and Salmonella typhi constituted one group of the same R-factor phenotype expressions. Most, but not all, penicillinase plasmids exhibited in Proteus PM1 a considerably lower order of beta-lactamase activity and an even lower order of resistance to the beta-lactam drugs than the previous two hosts. This difference was most pronounced for the resistance to carbenicillin, which was mediated by the plasmids specifying the synthesis of TEM-like enzymes. Release by osmotic shock was complete in the host E. coli K-12 for the TEM-like enzymes, but was lower for the cephalosporinase and minimal or negative in the PM1 host. Crypticity factor for benzylpenicillin, ampicillin, and carbenicillin was not related to the increase in resistance mediated by the penicillinase plasmids in both K-12 and PM1 hosts. Inoculum size effects for the penicillins and 6-aminopenicillanic acid were higher in PM1 than in K-12 R(+) cultures. The expression of penicillinase plasmids in wild-type bacteria was strain specific and not species specific. For two plasmids of different phenotypes for beta-lactamase activity (and resistance) in K-12 and PM1 hosts, a positive correlation was found between their phenotype and the relative amount of episomal deoxyribonucleic acid, as detected by ethidium bromide density gradient centrifugation. This is interpreted as indicating differences in the mode of replication of the plasmids in the two hosts.

Escherichia coli K12↗

The isolation and partial characterization of glycolipids of normal human leucocytes.

1. The lipids of purified human leucocytes were extracted with chloroform-methanol and the extract was washed with water. Glycolipids, isolated by Florisil chromatography, were subjected to mild alkaline hydrolysis and the alkali-resistant fraction was fractionated on a silicic acid column. 2. Three classes of glycolipid were separated. The less polar, containing 3.6% of the total glycolipid hexose as galactose, was tentatively identified as ceramide monohexoside. The major glycolipid fraction was characterized as ceramide dihexosides. The more polar glycolipids comprised 1.6% of the total glycolipid hexose as galactose and glucose (in the molar ratio 2:1) and were non-acidic. This class was separated as a mixture containing ninhydrin-positive glycolipids. 3. The ceramide dihexosides taken from two leucocyte preparations accounted for 15.2% and 16.4% by weight of the total lipids. 4. The carbohydrate moiety of the ceramide dihexosides contained galactose and glucose in the molar ratio 2:1. Partial acid hydrolysis and paper chromatography indicated that the hexoses are present as disaccharides, lactose being identified as one of them. 5. Palmitic acid (C(16:0)) and nervonic acid (C(24:1)) were the major fatty acids of this glycolipid. Hydroxy fatty acids were not detected.

Chemical Phenomena↗