Localization of recently characterized membrane transport adenosine triphosphatases

Na super(+), K super(+) -ATPase is the best-known member of a family of membrane transport ATPases sharing a number of structural features. Methods recently developed for Na super(+) K super(+) -ATPase localization may, therefore, be modifiable for use in studies of the distrubutions of related enzy...

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Veröffentlicht in:	The Histochemical journal 1981-07, Vol.13 (4), p.517-524
Hauptverfasser:	Firth, J A, Stranks, G J
Format:	Artikel
Sprache:	eng
Schlagworte:	4-Nitrophenylphosphatase - metabolism Adenosine Triphosphatases - metabolism adenosinetriphosphatase Animals Biological Transport, Active Cell Membrane - enzymology H(+)-K(+)-Exchanging ATPase Lead - metabolism localization Magnesium - metabolism methodology Mice plasma membranes Sodium-Potassium-Exchanging ATPase - metabolism Stomach - enzymology Strontium - metabolism
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Beschreibung
Zusammenfassung:	Na super(+), K super(+) -ATPase is the best-known member of a family of membrane transport ATPases sharing a number of structural features. Methods recently developed for Na super(+) K super(+) -ATPase localization may, therefore, be modifiable for use in studies of the distrubutions of related enzymes. Our experiences in the use of monophosphate and triphosphate substrate methods for localization of the gastric proton pump ATPase (H super(+), K super(+) -ATPase) are described and the prospects for localizing other related enzymes by similar techniques are discussed.
ISSN:	0018-2214 1573-6865
DOI:	10.1007/BF01002707