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

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)

Access to Document

10.1016/0024-3205(70)90080-9

Fingerprint Dive into the research topics of 'Localization of Na+K+, Mg++ adenos inetriphosphatase activity in pulmonary alveolar macrophage subcellular fractions'. Together they form a unique fingerprint.

Cite this

Mustafa, M. G., Cross, C. E., & Hardie, J. A. (1970). Localization of Na⁺K⁺, Mg⁺⁺ adenos inetriphosphatase activity in pulmonary alveolar macrophage subcellular fractions. Life Sciences, 9(16 PART 1), 947-954. https://doi.org/10.1016/0024-3205(70)90080-9

@article{7bef697d8e2a4a929e99b6a4603ec2c7,

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

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.",

author = "Mustafa, {Mohammad G.} and Cross, {Carroll E} and Hardie, {Jeanne A.}",

year = "1970",

month = aug,

day = "15",

doi = "10.1016/0024-3205(70)90080-9",

language = "English (US)",

volume = "9",

pages = "947--954",

journal = "Life Sciences",

issn = "0024-3205",

publisher = "Elsevier Inc.",

number = "16 PART 1",

}

TY - JOUR

T1 - Localization of Na+K+, Mg++ adenos inetriphosphatase activity in pulmonary alveolar macrophage subcellular fractions

AU - Mustafa, Mohammad G.

AU - Cross, Carroll E

AU - Hardie, Jeanne A.

PY - 1970/8/15

Y1 - 1970/8/15

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.

UR - http://www.scopus.com/inward/record.url?scp=0014948799&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0014948799&partnerID=8YFLogxK

U2 - 10.1016/0024-3205(70)90080-9

DO - 10.1016/0024-3205(70)90080-9

M3 - Article

C2 - 4249840

AN - SCOPUS:0014948799

VL - 9

SP - 947

EP - 954

JO - Life Sciences

JF - Life Sciences

SN - 0024-3205

IS - 16 PART 1

ER -