Abstract
1. By isoelectric focusing pig liver esterase (EC 3.1.1.1) is separated into 4 main, but still inhomogeneous peaks. A study of the specificity of these main variants, using acetanilide, methyl butyrate, and o-nitrophenyl acetate as substrates, showed that all 3 compounds were hydrolysed by all enzyme forms. The ratios of the activities, however, differed considerably. 2. Butyryl choline is hydrolysed by highly purified liver esterase, whereas liver esterases from ox and rat are inactive toward this substrate. The activity of pig liver esterase toward butyryl choline and methyl butyrate is completely inhibited by 10 µM physostigmine. 3. The present state of knowledge on the main molecular properties of pig liver esterase is reviewed. The available evidence strongly suggests that the enzyme is a trimer. 4. A comparison is made of the structure of 5 carboxylesterase preparations of different origin. 5. Some current problems on the nomenclature and classification of carboxylesterases are discussed in the light of recent findings from our laboratory.
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