PROPERTIES OF MONOAMINE OXIDASES IN SYMPATHETIC NERVE AND PINEAL GLAND

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Abstract
Abstract— The monoamine oxidases (MAO) of rat pineal gland and superior cervical ganglion were compared and found to have different characteristics. The predominant enzyme in the ganglion was inhibited by low concentrations of clorgyline (0.1 μM), exhibited a lower apparent Km for tyramine than the enzyme in the pineal, was readily inactivated by trypsin, and was relatively heat‐stable. In contrast, the MAO of the pineal was inhibited by 0.1 mm clorgyline, was not readily inactivated by trypsin, and was heat‐labile. Moreover, these enzymes appeared to have different substrate specificities. Our results are consistent with the view that there may be multiple forms of MAO and that these forms may be associated with specific cell types.