Linked Life Data

7452967

Source:http://linkedlifedata.com/resource/pubmed/id/7452967

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-3-27
pubmed:abstractText
The activity of mitochondrial monoamine oxidase (MAO) from human placenta was measured with mixtures of labelled and unlabelled tyramine, serotonin (5-HT), benzylamine and beta-phenylethylamine (PEA). Tyramine deamination was inhibited by benzylamine and PEA but not by 5-HT, while benzylamine deamination was inhibited by tyramine and PEA, but not by 5-HT, 5-HT deamination was inhibited by tyramine, benzylamine and PEA and PEA deamination was inhibited by tyramine, benzylamine and 5-HT. These results suggest that MAO in human placenta has multiple catalytic sites or consists of different enzymes. Probably, tyramine, benzylamine and PEA are deaminated oxidatively at a common catalytic site while 5-HT is deaminated at another catalytic site. Benzylamine deamination was inhibited in a mixed noncompetitive fashion by tyramine and PEA in air, but benzylamine deamination was competitively inhibited by PEA at higher concentrations of oxygen. The deaminations of other substrates were inhibited competitively by other substrates, in air. Reciprocal plots of PEA deamination with benzylamine, 5-HT and tyramine gave hyperbolic curves.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-5198
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-64
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Studies on human placental monoamine oxidase using mixed substrates.
pubmed:publicationType
Journal Article