Phosphorylated intermediate of the ATPase of plant plasma membranes

A partially purified preparation of the plant plasma membrane ATPase was phosphorylated when incubated with [gamma-32P]ATP. The phosphoprotein formed has the characteristics of an enzyme intermediate because of its rapidity of phosphorylation and dephosphorylation. The sensitivity of the phosphoenzy...

Full description

Saved in:
Bibliographic Details
Published inThe Journal of biological chemistry Vol. 258; no. 9; pp. 5334 - 5336
Main Authors Vara, F, Serrano, R
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 10.05.1983
American Society for Biochemistry and Molecular Biology
Subjects
Adenosine Triphosphatases - metabolism
Cell Membrane - enzymology
Electrophoresis, Polyacrylamide Gel
Hydroxylamine
Hydroxylamines - pharmacology
Kinetics
Phosphorylation
Plants - enzymology
Online AccessGet full text

Cover

More Information
Summary:A partially purified preparation of the plant plasma membrane ATPase was phosphorylated when incubated with [gamma-32P]ATP. The phosphoprotein formed has the characteristics of an enzyme intermediate because of its rapidity of phosphorylation and dephosphorylation. The sensitivity of the phosphoenzyme bond to alkaline pH and to hydroxylamine indicates that it is an acylphosphate. Both the ATPase activity and the phosphorylation of the enzyme exhibited an apparent Km value of 0.3 mM ATP. When the phosphorylated enzyme was analyzed by electrophoresis in sodium dodecyl sulfate, only one major band with a molecular weight of about 105,000 contained radioactivity. These results indicate that the plant plasma membrane ATPase has a subunit composition and reaction mechanism similar to the cation-pumping ATPases of animal and fungal plasma membranes.
Bibliography:F60
F
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(20)81890-0