PLASMALOGENASE IN HAMSTER HEART

The presence of plasmalogenase for the hydrolysis of the alk-1-enyl bond at the C-1 position of 1-alkenyl-2-acyl-sn-glycero-3-phosphoethanolamine (ethanolamine plasmalogens) in the hamster heart was examined. A new spectrophotometric assay was developed, in which the aldehyde released by the hydrolysis of the plasmalogenase was oxidized to carboxylic acid by the action of aldehyde dehydrogenase, with the production of the molar equivalent of NADH. The results obtained from the spectrophotometric assay were comparable to those obtained by determining the rate of ethanolamine plasmalogens utilized during the reaction. The sensitivity of the spectrophotometric assay for plasmalogenase was shown to be 25-fold higher than with the methods described previously and enzyme activity could be detected with 1 .mu.g of microsomal protein. Hamster heart plasmalogenase activity was located exclusively in the microsomal fraction, and the enzyme displayed a pH optimum at 8.5. The enzyme showed no absolute requirement for divalent metallic cations.