Abstract
The enzymes which hydrolyze isopropyl methylphosphonofluoridate (sarin) and ethyl N, N-dimethylphosphoramidocyanidate (tabun) have been studied. Michaelis–Menten constants and activation energies have been estimated and enzyme stability has been studied. The distribution of the enzymes in mammalian tissues has been examined. It is concluded that from each source the same enzyme is responsible for the hydrolysis of sarin and tabun but that this enzyme shows variations from source to source. That there are mixtures of very similar enzymes, having a composition in amounts characteristic of the source, is also considered possible.
Publisher
Canadian Science Publishing
Cited by
6 articles.
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