Linked Life Data

1529792

Source:http://linkedlifedata.com/resource/pubmed/id/1529792

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
1992-10-16
pubmed:abstractText
In rat lung microsomes, an enzyme showing high histaminase activity is present. The oxidation of histamine is dependent on the presence of two enzymic activities, both inhibited by alpha-aminoguanidine and by B24, an inhibitor of semicarbazide-sensitive amine oxidases (SSAO) which have benzylamine as preferential substrate. These enzymic activities differ in substrate specificity: one appears to be a classical tissue bound SSAO enzyme with high affinity for benzylamine, the other a diamine oxidase (DAO) with properties that are very different from the classical DAO. This latter enzyme is not inhibition by high histamine concentrations and is more active at pH 8.5 than at pH 7.4.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0065-4299
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
192-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Histaminase activity in rat lung and its comparison with intestinal mucosal diamine oxidase.
pubmed:affiliation
Department of Preclinical and Clinical Pharmacology M. Aiazzi Mancini, University of Florence, Firenze, Italy.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't