Purification and properties of dialkylfluorophosphatase
article
1. 1. Zone electrophoresis on starch columns of purified preparations of fluorophosphatase resulted in a further purification. The preparations thus obtained differed in various respects from the cruder ones so far described. 2. 2. In the course of this electrophoresis fractions were obtained, which, although themselves almost or entirely lacking enzymic activity, could activate the enzyme. This activation was particularly impressive when studied in the presence of Mn++ ions. The activation is very marked when DFP is used as a substrate. In the case of other substrates, the activation usually also occurs although it is less marked. 3. 3. Mn++ ions activate the hydrolysis of DFP and tabun but inhibit that of most other substrates. 4. 4. p-Chloromercuribenzoic acid inhibits the enzyme. This inhibition is wholly or partially reversible by cysteïne. 5. 5. The hydrolysis was studied with a number of substrates. It is probably due to one and the same enzyme, present in the purified preparations, although the possibility that the hydrolysis of tabun requires a second enzyme could not be excluded. 6. 6. Intravenous injection of DFPase preparations afforded a certain amount of protection in rats when given previous to lethal dosages of DFP or sarin. © 1957.
TNO Identifier
226667
ISSN
00063002
Source
BBA - Biochimica et Biophysica Acta, 26(1), pp. 29-39.
Pages
29-39
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