Linked Life Data

8885413

Source:http://linkedlifedata.com/resource/pubmed/id/8885413

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1997-1-23
pubmed:abstractText
The presence and activities of the enzymes of the urea cycle in the bacterium Helicobacter pylori were investigated employing one- and two-dimensional NMR spectroscopy and radioactive tracer analysis. Cell suspensions, lysates and membrane preparations generated L-ornithine and ammonium at high rates in incubations with L-arginine, indicating the presence of arginase activity. Anabolic ornithine transcarbamoylase (OTCase) activity was identified by the formation of heat-stable products in incubations of cell-free extracts with ornithine and radiolabelled carbamoyl phosphate. The heat-labile product that resulted from incubations of cell-free extracts with citrulline radiolabelled in the guanidino moiety revealed the presence of catabolic OTCase activity. Argininosuccinate formation and catalysis indicated the presence of argininosuccinate synthetase and argininosuccinase activities. The findings suggested that H. pylori has a urea cycle which acts as an effective mechanism to extrude excess nitrogen from cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1350-0872
pubmed:author
pubmed:issnType
Print
pubmed:volume
142 ( Pt 10)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2959-67
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
The urea cycle of Helicobacter pylori.
pubmed:affiliation
School of Biochemistry, University of New South Wales, Sydney, Australia. G.Mendz@unsw.EDU.AU
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't