Linked Life Data

2866915

Source:http://linkedlifedata.com/resource/pubmed/id/2866915

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1986-2-20
pubmed:abstractText
Monoamine oxidase (MAO) activity was measured in ring dove (Streptopelia risoria) tissues using a fluorometric assay with kynuramine as substrate. Harmaline inhibited MAO activity in a time-dependent manner, and preincubation of enzyme with the drug did not affect its activity. Pargyline produced a slow-onsetting inhibition of activity which was enhanced by preincubation of enzyme and inhibitor. Harmaline displayed reversible non-competitive inhibition of MAO activity. Oxygen is also a substrate for dove MAO, and the reaction apparently involves "ping-pong", double-displacement kinetics. Dove MAO activity is temperature-dependent, with an activation energy of 13.1 kcal/mole.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0742-8413
pubmed:author
pubmed:issnType
Print
pubmed:volume
82
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
417-22
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Biochemistry and physiology of monoamine oxidase (MAO) activity in the ring dove (Streptopelia risoria). I. Characteristics of MAO activity in vitro.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't