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Biomedical subjects

E Willoughby

Publications and source records attributed to E Willoughby.

13 recordsLinked to original sources
PubMed1978

Coma in the Wernicke-Korsakoff syndrome.

Four comatose patients were found to have the Wernicke-Krosakoff syndrome. All had a history of alcoholism, previous alcoholic neurological disease, and poor nutrition. Intravenous or nasogastric tube feeding without vitamin supplements precipitated coma in three. Examination showed a diffuse encephalopathy with intact pupillary light reflexes, no focal neurological signs, and absent doll's eye and caloric responses. The tendon reflexes were uniformly absent. Two patients were hypothermic and one was hypotensive. Although the level of consciousness improved in all after parenteral thiamine, three died and one was left disabled. The Wernicke-Korsakoff syndrome merits wider recognition as a cause of coma and empirical treatment with thiamine in cases of coma of unknown cause is recommended.

Coma↗
PubMed1977

Hydroxylaminolysis of penicillin binding componenets is enzymatically catalyzed.

The hydroxylaminolysis of the penicilloyl moiety from [14C]penicillin G binding component (PBC) complexes of the Bacillus subtilis D-alanine carboxypeptidase and of the mixture of PBC's of Staphylococcus aureus was inhibited by denaturation of the complexes by heat (55 degrees), detergent (1% sodium dodecyl sulfate), or trichloroacetic acid. The kinetics of inhibition by denaturation were comparable to those of the inhibition of [14C]penicillin G binding to the PBC's and of carboxypeptidase activity of the B. subtilis enzyme under identical denaturing conditions. These data establish that the hydroxylaminolysis is an enzymatically catalyzed process suggesting that penicillin G is bound to an enzymatically active site. Treatment of the denatured [14C]penicillin G-carboxypeptidase complex with sodium borohydride or at pH 12 resulted in the release of the penicilloyl moiety. These results are consistent with a carboxylic ester bond for the penicilloyl-PBC instead of a thiolester linkage as was initially presumed.

Alanine↗
PubMed1974

Mechanism of action and development of resistance to a new amidino penicillin.

The mechanism of killing of Escherichia coli by a novel beta-lactam antibiotic, an amidino penicillin, has been investigated. This compound converts E. coli to relatively stable spherical forms at low concentration. However, the amidino penicillin caused no alteration in any of those parameters of peptidoglycan synthesis which can be studied. Above 10 mug of the antibiotic per ml the cells began to lyse, and a second mode of killing appeared. Mutants resistant to the amidino penicillin were isolated and several were studied in detail. Three mutant phenotypes were distinguished: (i) spherical shape and hypersensitive to lysis by either amidino penicillin or ampicillin; (ii) spherical shape and normally sensitive to lysis; (iii) rod shape, converted to viable spheres by amidino penicillin and normally sensitive to lysis.

Amidines↗