Linked Life Data

18400766

Source:http://linkedlifedata.com/resource/pubmed/id/18400766

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-7-8
pubmed:abstractText
A bacterial semicarbazide-sensitive amine oxidase (SSAO) was purified and characterized from Mycobacterium sp. strain JC1 DSM 3803 grown on benzylamine. During the purification procedures, the enzyme was tending to aggregate and exhibited heterogeneity in native PAGE. The heterogeneous forms having amine oxidase (AO) activity could be separated by their native molecular weights using gel-filtration chromatography. Most of the AOs behaved as dimers (M(r) 150,000) composed of a 75-kDa subunit, but some aggregated to form tetramers (M(r) 300,000). Besides their native molecular weight, subunit composition and V(max) value, both forms (dimer and tetramer) have almost identical biochemical properties (e.g. subunit size, optimum pH and temperature, activation energy, K(m) value on benzylamine, substrate and inhibitor specificities). When AO activity was observed by activity staining, the best-oxidized substrate was benzylamine, although the AO also oxidized tyramine and histamine. The AO was strongly inhibited by semicarbazide and isoniazid, but KCN did not affect its activity. The purified enzyme was shown to contain 2.39 mol of copper per mole of subunit, but there were no evidences of topaquinone co-factor involvement, when tested by absorption spectrum analysis and redox-cycling staining for quinoprotein detection.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
144
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
107-14
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Purification and characterization of a copper-containing amine oxidase from Mycobacterium sp. strain JC1 DSM 3803 grown on benzylamine.
pubmed:affiliation
Laboratory of Biochemistry, Graduate School of Medicine, Konkuk University, Chungju 380-701, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't