Penicillin Site of Action
- 28 February 1947
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 105 (2722) , 235-236
- https://doi.org/10.1126/science.105.2722.235
Abstract
Polemic with C. S. Leonard. He assumes that all agents which inhibit growth by interaction with -SH groups should have more or less equal toxic manifestations in animals and should inhibit the same types of organisms. This implies that there is only one type of SH-active enzyme in all spp. and that only one type of reaction occurs with the inhibitor. The available evidence shows that these assumptions are not true. Cavallito observed antibiotics for reactivity with thiols in vitro and minimized in vivo tests. The relevance of thioglycolate stimulation of penicillinase action or oi the rapid excretion of penicillin to the mechanism of action of penicillin is not evidence for or against a sulfhydryl inhibition mechanism. It is not essential that penicillin should bind protein -SH in direct proportion to the number of -SH groups in proteins since some types of these groups react sluggishly or not at all with penicillin.Keywords
This publication has 5 references indexed in Scilit:
- Lack of Influence of Thiosulfate and Metabisulfite on the Antibiotic Activity of PenicillinScience, 1946
- RELATIONSHIP OF THIOL STRUCTURES TO REACTION WITH ANTIBIOTICSJournal of Biological Chemistry, 1946
- STUDIES ON BIOLOGICAL OXIDATIONSPublished by Elsevier ,1945
- STUDIES ON BIOLOGICAL OXIDATIONSJournal of Biological Chemistry, 1945