Linked Life Data

11008875

Source:http://linkedlifedata.com/resource/pubmed/id/11008875

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-1-22
pubmed:abstractText
In guinea pig dorsal skin the semicarbazide-sensitive amine oxidase (SSAO) is localised in fibroblasts. Fibroblasts in culture lose the ability to express this enzymatic activity with doublings, thus suggesting that the SSAO expression needs some factors which are not present in the 10% bovine serum culture medium. Fresh bovine serum of adult animals contains two SSAO activities, one with high affinity for benzylamine and one with lower affinity. The enzyme with lower affinity for benzylamine was identified as spermine oxidase, the oxidation of [14C]-benzylamine was inhibited by semicarbazide, alpha-aminoguanidine and B24, a specific inhibitor of benzylamine oxidase and spermine oxidase, both SSAO enzymes. The enzymatic activity of bovine serum was partially purified, the kinetic properties and sensitivity to inhibitors studied. A mathematical procedure for the analysis of the kinetics resulting from the activity of two enzymes acting on the same substrate seems to give better results than the methods previously described.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1216-8068
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17-35
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Semicarbazide-sensitive amine oxidases in heart and bovine serum.
pubmed:affiliation
Department of Pharmacology of the University of Florence, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't