Abstract
Conditions were established for using the 4-aminoantipyrine reagent for following the course of enzymic hydrolysis of some aromatic esters. Employing this chromogenic reagent, it was found that plasmata from 15 species were active in the liberation of 1-naphthol from 1-naphthyl N-methylcarbamate (the insecticide, Sevin). Rabbit plasma was more active in this respect than comparable fresh weights of 16 other rabbit tissues. Plasmata from 8 species were fractionated by column electrophoresis and the activity in liberation of 1-naphthol from Sevin was found to be associated in every case with the albumin and not with the aromatic, aliphatic or choline esterases. On low temperature ethanol fractionation of human serum, the activity in liberating 1-naphthol from Sevin appeared entirely in the albumin component (Fraction V). Certain aromatic acetates also reacted with plasma (serum) albumin, apparently in an analogous manner to the reaction of Sevin. The kinetics were investigated for the reaction of 1-naphthyl and p-nitrophenyl acetates and N-methyl-carbamates with human serum albumin. The similarity of albumin in reacting with these esters to an “esterase” is discussed.
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