A. K. Balls

Learn More
Diisopropyl fluorophosphate (DFP) has been shown to be a remarkably potent inhibitor of the enzymatic hydrolysis of acetylcholine (1). As a result of a wide survey (2), inhibition by dialkyl fluorophosphates appears to be specific for certain esterases and lipases (kidney acid phosphatase was found to be inhibited by relatively high concentrations). Since(More)
Although the milk-clotting action of papain has been recognized for many years, this property of the enzyme has received little quantitative attention. It appears to be, however, a characteristic property of the proteolytic component of this enzyme system. Various workers have brought forth evidence as to the composite nature of the papain system, which has(More)
The isolation of crystalline ar-amylase has been reported in a preliminary communication (1). Details of the method of isolation, behavior of the fractions leading to crystallization, and some properties of the crystalline material are reported here. This material constitutes the first instance of the crystallization of an cu-amylase from a higher plant and(More)
The introduction of one acetyl group into the chymotrypsin molecule by reaction with p-nitrophenyl acetate gives rise to an enzymatically inactive monoacetylated protein that rapidly loses its acetyl group and becomes active again in solutions of dilute alkali or primary alcohols." 2 On the other hand, the well-known polyacetylation of proteins with acetic(More)