Linked Life Data

6120995

Source:http://linkedlifedata.com/resource/pubmed/id/6120995

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1982-5-27
pubmed:abstractText
We have investigated the properties of several ATPases present in synaptic membrane preparations from the cerebral cortex of rat. In addition to the intrinsic (Na+ + K+)-ATPase and a low level of contaminating Mg2+-ATPase of mitochondrial origin, both of which could be controlled by the addition of ouabain and azide, respectively, four activities were studied: (1) a Mg2+-ATPase; (2) a Mg2+-independent activity requiring Ca2+ ions at high concentrations; (3) a (Ca2+ + Mg2+)-ATPase with a high affinity for Ca2+, which were enhanced further (4) by the inclusion of calmodulin (33 nM for half-maximal activity). In the presence of 0.5 mM-EGTA in the buffer used, half saturation for these respective metal ions was observed at 0.9 mM for (1), 1.0 mM for (2), and approximately 0.3 mM for (3) and (4); the latter values correspond to concentrations of free Ca2+ of 0.38 and 0.18 microM for (3) and (4), respectively. The level of activities observed, all in nmol X min-1 X mg-1, under optimal conditions of 37 degrees C, was in a number of preparations (n in parenthesis): for (1) 446 +/- 19 (19); for (2) 362 +/- 18 (3) for (3) 87 +/- 13 (12); and for (4) 161 +/- 29 (12). The (Ca2+ + Mg2+)-ATPase, both in the presence and absence of calmodulin, could be inhibited specifically by a number of agents (approximate I0.5 in parentheses) which, at these concentrations, showed little or no potency against the other activities; among them were vanadate (less than or equal to 10 microM), La3+ (75 microM), trifluoperazine, and other phenothiazines (50 microM). These properties suggest that the (Ca2+ + Mg2+)-ATPase described may be responsible for calcium transport across one (or more) of the several membranes present in nerve endings and contained in the preparation used.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1407-18
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Calcium-stimulated adenosine triphosphatases in synaptic membranes.
pubmed:publicationType
Journal Article