The esterases of horse blood. 2. The specificity of horse erythrocyte cholinesterase
- 1 November 1950
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 47 (5) , 525-530
- https://doi.org/10.1042/bj0470525
Abstract
Horse erythrocyte cholinesterase was partially purified and freed from ali-esterase by a new method. In its specificity and physical behavior it closely resembles human erythrocyte cholinesterase. It hydrolyzes a number of aliphatic esters, the rates of hydrolysis of these substrates being higher the nearer the structure of acetycholine is approached. The carbon analog of acetylcholine (3, 3-dimethyl-butyl acetate) has the highest rate of hydrolysis of any simple aliphatic ester so far examined. The results are discussed in relation to the general question of cholinesterase specificity.Keywords
This publication has 4 references indexed in Scilit:
- The esterases of horse blood. 1. The specificity of horse plasma cholinesterase and ali-esteraseBiochemical Journal, 1950
- Studies on cholinesteraseBiochemical Journal, 1943
- Studies on cholinesteraseBiochemical Journal, 1943
- Blood esterasesBiochemical Journal, 1942