Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
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Gene/Protein
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Target Concepts:
Gene/Protein
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Query: EC:3.6.3.1 (
Mg2+-ATPase
)
1,484
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
A procedure is described for the preparation of a membrane fraction enriched in basal-lateral plasma membranes from gastric mucosa. Gastric glands isolated from rabbit were employed as starting material, greatly reducing contamination from non-glandular cell types. The distribution of cellular components during the fractionation procedure was monitored with specific marker enzymes. (Na+ + K+)-ATPase, ouabain-sensitive K+-stimulated p-nitrophenyl-phosphatase and histamine-stimulated adenylate cyclase were used as markers for basal-lateral membranes. These three markers were similarly distributed during both differential and equilibrium density gradient centrifugation. The enriched membrane fraction contained more than 30% of the total initial activities of the three basal-lateral membrane markers which were purified better than 11-fold with respect to protein. (Na+ + K+)-ATPase activity was resolved from the activities of acid phosphatase, pepsin,
Mg2+-ATPase
, cytochrome c oxidase, NADPH-cytochrome c reductase, glucose-6-phosphatase,
(K+ + H+)-ATPase
, DNA and RNA.
...
PMID:An enriched preparation of basal-lateral plasma membranes from gastric glandular cells. 626 84
(1) A
(K+ + H+)-ATPase
containing membrane fraction, isolated from pig gastric mucosa, has been further purified by means of zonal electrophoresis, leading to a 20% increase in specific activity and an increase in ratio of
(K+ + H+)-ATPase
to basal
Mg2+-ATPase
activity from 9 to 20. (2) The target size of (Na+ + K+)-ATPase, determined by radiation inactivation analysis, is 332 kDa, in excellent agreement with the earlier value of 327 kDa obtained from the subunit composition and subunit molecular weights. This shows that the Kepner-Macey factor of 6.4 X 10(11) is valid for membrane-bound ATPases. (3) The target size of
(K+ + H+)-ATPase
is 444 kDa, which, in connection with a subunit molecular weight of 110000, suggests a tetrameric assembly of the native enzyme. The ouabain-insensitive K+-stimulated p-nitrophenylphosphatase activity has a target size of 295 kDa. (4) In the presence of added Mg2+ the target sizes of the
(K+ + H+)-ATPase
and its phosphatase activity are decreased by about 15%, while that for the (Na+ + K+)-ATPase is not significantly changed. This observation is discussed in terms of a Mg2+-induced tightening of the subunits composing the
(K+ + H+)-ATPase
molecule.
...
PMID:Studies on (K+ + H+)-ATPase. VI. Determination on the molecular size by radiation inactivation analysis. 630 21