Date of Award

1974

Degree Type

Thesis

Degree Name

Master of Science (MS)

Department

Biological Sciences

Abstract

Brain homogenates of the honeybee, Apis mellifera, have been found to possess enzymes capable of catalyzing the N-acetylation of tryptamine and 5-hydroxytryptamine with acetyl coenzyme A as the acetyl donor. The Km of the N-acetylation of tryptamine was 5. 0 x 10-7 M at iii pH 7. 0 and 33°C. Evidence was obtained that the indolealkylamines, tryptamine and 5-hydroxytryptamine, are not oxidized by monoamine oxidase (MAO) as is commonly considered to be a major catabolic route in vertebrate animals. Certain commonly used assays, reportedly specific for monoamine oxidase activity, will not distinguish between oxidation by MAO and N-acetylation of tryptamine and so should not be used to assay for MAO activity in insect tissues without careful identification of the products of the reaction. Implications of N-acetylation of indolealkylamines are discussed in relation to the neurotransmitter problem.

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