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dc.contributor.authorEvans, Philip Harold
dc.date.accessioned2021-09-07T22:27:15Z
dc.date.available2021-09-07T22:27:15Z
dc.date.issued1/1/1974
dc.identifier.urihttp://hdl.handle.net/20.500.12648/6407
dc.description.abstractBrain 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.
dc.subjectThesis 167
dc.subjectBrockport Thesis Collection
dc.subjectHoney Bee
dc.subjectEnzyme
dc.subjectMao
dc.subjectBTC
dc.titleEnzymatic N-Acetylation of Indolealkylamines by Brain Homogenates of the Honeybee, Apis Mellifera
dc.typethesis
refterms.dateFOA2021-09-07T22:27:15Z
dc.description.institutionSUNY Brockport
dc.description.departmentBiological Sciences
dc.description.degreelevelMaster of Science (MS)
dc.source.statuspublished
dc.description.publicationtitleEnvironmental Science and Ecology Theses
dc.contributor.organizationThe College at Brockport
dc.languate.isoen_US


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