Linked Life Data

8829218

Source:http://linkedlifedata.com/resource/pubmed/id/8829218

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5-6
pubmed:dateCreated
1996-12-12
pubmed:abstractText
In a previous study we demonstrated the existence of a tightly-bound ATPase in the human placental mitochondria (Martínez et al., 1993). The current study characterizes the ATP hydrolysis produced by the F1F0-ATPase and the tightly-bound ATPase in submitochondrial particles from the human term placenta. Both enzymes were not differentiated by pH. Inhibitors were necessary to distinguish the activity of each enzyme. The kinetic of the total ATP hydrolysis fitted into a model of two enzymes. During the characterization, it was observed that the tightly-bound ATPase activity was partially inhibited by vanadate and Mg2+, whereas the F1F0-ATPase was totally inhibited by Mg2+. Different nucleotides were hydrolyzed by the tightly-bound ATPase; the F1F0-ATPase hydrolyzed exclusively ATP. Glucose-6-phosphate, p-nitrophenylphosphate, or pyrophosphate were not hydrolyzed by the F1F0-ATPase, although some hydrolysis was observed with the tightly-bound ATPase. It is concluded that the tightly-bound ATPase activity corresponded to a 5'-nucelotidase, and that the human placental mitochondria could participate in the metabolism of nucleotides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0143-4004
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
345-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Characterization of the F1F0-ATPase and the tightly-bound ATPase activities in submitochondrial particles from human term placenta.
pubmed:affiliation
Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, México D.F.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't