Untersuchungen über esterspaltende Enzyme von Versuchstieren und Methoden zu ihrer routinemäßigen Bestimmung, III. Einwertige Monoester hydrolysierende Enzyme im Rattenblut unter besonderer Berücksichtigung der Acetylcholinesterasen

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Abstract
Hemolytic rat serum and rat plasma were investigated for the presence of enzymes that hydrolyze monovalent aliphatic monoesters. Four such enzymes were isolated by preparative starch gel electrophoresis. Two of these were specific acetylcholinester-ases, which differed in their pH-optimum and electrical charge. The other 2 were unspecific enzymes, whose specificity range was studied with the aid of a wide range of substrates. Both of the unspecific enzymes hydrolyze choline esters with the exception of acetylcholine and succi-nyl choline esters. The optimum chain length for different esterified fatty acids, and the pH-optima for the cleavage of these esters by the unspecific enzymes are reported. Finally, by using the buffer system Tris-acetic acid with the starting material. 2 pH-optima were found for the cleavage of acetyl choline, which corresponded to the 2 acetyl cholinesterases. These were not found with other buffer systems.