Localization of Na+K+, Mg++ adenos inetriphosphatase activity in pulmonary alveolar macrophage subcellular fractions

Mohammad G. Mustafa; Carroll E Cross; Jeanne A. Hardie

doi:10.1016/0024-3205(70)90080-9

Localization of Na⁺K⁺, Mg⁺⁺ adenos inetriphosphatase activity in pulmonary alveolar macrophage subcellular fractions

Mohammad G. Mustafa, Carroll E Cross, Jeanne A. Hardie

Pulmonary, Critical Care, and Sleep Medicine

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Pulmonary alveolar macrophages manifest a Mg⁺⁺ dependent Na⁺-K⁺ stimulated ATPase activity. A survey of ATP hydrolyzing activity in various subcellular fractions reveals that the maximal activity is found in a fraction containing predominantly the macrophage plasma membrane. This Na⁺K⁺, Mg⁺⁺ ATPase is sensitive to ouabain and p-chloromercuribenzoate but insensitive to oligomycin. This enzyme system may be related to energy-dependent membrane-linked processes of alveolar macrophages.

Original language	English (US)
Pages (from-to)	947-954
Number of pages	8
Journal	Life Sciences
Volume	9
Issue number	16 PART 1
DOIs	https://doi.org/10.1016/0024-3205(70)90080-9
State	Published - Aug 15 1970

ASJC Scopus subject areas

Pharmacology
Medicine(all)

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abstract = "Pulmonary alveolar macrophages manifest a Mg++ dependent Na+-K+ stimulated ATPase activity. A survey of ATP hydrolyzing activity in various subcellular fractions reveals that the maximal activity is found in a fraction containing predominantly the macrophage plasma membrane. This Na+K+, Mg++ ATPase is sensitive to ouabain and p-chloromercuribenzoate but insensitive to oligomycin. This enzyme system may be related to energy-dependent membrane-linked processes of alveolar macrophages.",

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AU - Cross, Carroll E

AU - Hardie, Jeanne A.

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N2 - Pulmonary alveolar macrophages manifest a Mg++ dependent Na+-K+ stimulated ATPase activity. A survey of ATP hydrolyzing activity in various subcellular fractions reveals that the maximal activity is found in a fraction containing predominantly the macrophage plasma membrane. This Na+K+, Mg++ ATPase is sensitive to ouabain and p-chloromercuribenzoate but insensitive to oligomycin. This enzyme system may be related to energy-dependent membrane-linked processes of alveolar macrophages.

AB - Pulmonary alveolar macrophages manifest a Mg++ dependent Na+-K+ stimulated ATPase activity. A survey of ATP hydrolyzing activity in various subcellular fractions reveals that the maximal activity is found in a fraction containing predominantly the macrophage plasma membrane. This Na+K+, Mg++ ATPase is sensitive to ouabain and p-chloromercuribenzoate but insensitive to oligomycin. This enzyme system may be related to energy-dependent membrane-linked processes of alveolar macrophages.

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