Enzymatic N-Acetylation of Indolealkylamines by Brain Homogenates of the Honeybee, Apis Mellifera
dc.contributor.author | Evans, Philip Harold | |
dc.date.accessioned | 2021-09-07T22:27:15Z | |
dc.date.available | 2021-09-07T22:27:15Z | |
dc.date.issued | 1974-01-01 | |
dc.identifier.uri | http://hdl.handle.net/20.500.12648/6407 | |
dc.description.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. | |
dc.subject | Thesis 167 | |
dc.subject | Brockport Thesis Collection | |
dc.subject | Honey Bee | |
dc.subject | Enzyme | |
dc.subject | Mao | |
dc.subject | BTC | |
dc.title | Enzymatic N-Acetylation of Indolealkylamines by Brain Homogenates of the Honeybee, Apis Mellifera | |
dc.type | thesis | |
refterms.dateFOA | 2021-09-07T22:27:15Z | |
dc.description.institution | SUNY Brockport | |
dc.description.department | Biological Sciences | |
dc.description.degreelevel | Master of Science (MS) | |
dc.source.status | published | |
dc.description.publicationtitle | Environmental Science and Ecology Theses | |
dc.contributor.organization | The College at Brockport | |
dc.languate.iso | en_US |