Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1981 Sep;68(3):521–526. doi: 10.1104/pp.68.3.521

Characterization of ATPase Activity Associated with Corn Leaf Plasma Membranes 1

David S Perlin 1,2, Roger M Spanswick 1
PMCID: PMC425932  PMID: 16661950

Abstract

A Mg2+-dependent, cation-stimulated ATPase was associated with plasma membranes isolated from corn leaf mesophyll protoplasts. Potassium was the preferred monovalent cation for stimulating the ATPase above the Mg2+-activated level. The enzyme was substrate-specific for ATP, was inhibited by N,N′-dicyclohexylcarbodiimide, diethylstilbestrol, p-chloromercuribenzoate, and orthovanadate, but was insensitive to oligomycin or sodium azide. A Km of 0.28 millimolar Mg2+-ATP was determined for the K+-ATPase, and the principal effect of potassium was on the Vmax for ATP hydrolysis. Since potassium stimulation was not saturated at high concentrations, a nonspecific role was proposed for potassium stimulation. A nonspecific phosphatase was also found to be associated with corn leaf plasma membranes. However, it could not be determined positively whether this activity represented a separate enzyme.

The cation-stimulated ATPase of corn leaves is biochemically similar to other plant plasma membrane enzymes. Thus, the ATPase can serve as a reliable qualitative plasma membrane marker providing its activity is well characterized.

Full text

PDF
523

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Balke N. E., Hodges T. K. Comparison of Reductions in Adenosine Triphosphate Content, Plasma Membrane-associated Adenosine Triphosphatase Activity, and Potassium Absorption in Oat Roots by Diethylstilbestrol. Plant Physiol. 1979 Jan;63(1):53–56. doi: 10.1104/pp.63.1.53. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Balke N. E., Hodges T. K. Plasma membrane adenosine triphosphatase of oat roots: activation and inhibition by mg and ATP. Plant Physiol. 1975 Jan;55(1):83–86. doi: 10.1104/pp.55.1.83. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boss W. F., Ruesink A. W. Isolation and Characterization of Concanavalin A-labeled Plasma Membranes of Carrot Protoplasts. Plant Physiol. 1979 Dec;64(6):1005–1011. doi: 10.1104/pp.64.6.1005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bowman B. J., Slayman C. W. Characterization of plasma membrane adenosine triphosphatase of Neurospora crassa. J Biol Chem. 1977 May 25;252(10):3357–3363. [PubMed] [Google Scholar]
  5. Dupont F. M., Burke L. L., Spanswick R. M. Characterization of a partially purified adenosine triphosphatase from a corn root plasma membrane fraction. Plant Physiol. 1981 Jan;67(1):59–63. doi: 10.1104/pp.67.1.59. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Grubmeyer C., Spencer M. Oligomycin-sensitive ATPase of Submitochondrial Particles from Corn. Plant Physiol. 1978 Apr;61(4):567–569. doi: 10.1104/pp.61.4.567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hendrix D. L., Kennedy R. M. Adenosine triphosphatase from soybean callus and root cells. Plant Physiol. 1977 Feb;59(2):264–267. doi: 10.1104/pp.59.2.264. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hodges T. K., Leonard R. T., Bracker C. E., Keenan T. W. Purification of an ion-stimulated adenosine triphosphatase from plant roots: association with plasma membranes. Proc Natl Acad Sci U S A. 1972 Nov;69(11):3307–3311. doi: 10.1073/pnas.69.11.3307. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. KACHMAR J. F., BOYER P. D. Kinetic analysis of enzyme reactions. II. The potassium activation and calcium inhibition of pyruvic phosphoferase. J Biol Chem. 1953 Feb;200(2):669–682. [PubMed] [Google Scholar]
  10. Leonard R. T., Hodges T. K. Characterization of Plasma Membrane-associated Adenosine Triphosphase Activity of Oat Roots. Plant Physiol. 1973 Jul;52(1):6–12. doi: 10.1104/pp.52.1.6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Leonard R. T., Hotchkiss C. W. Cation-stimulated Adenosine Triphosphatase Activity and Cation Transport in Corn Roots. Plant Physiol. 1976 Sep;58(3):331–335. doi: 10.1104/pp.58.3.331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lurie S. Differential Ion Stimulation of Plasmalemma Adenosine Triphosphatase from Leaf Epidermis and Mesophyll of Nicotiana rustica L. Plant Physiol. 1979 May;63(5):936–939. doi: 10.1104/pp.63.5.936. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Markwell M. A., Haas S. M., Bieber L. L., Tolbert N. E. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem. 1978 Jun 15;87(1):206–210. doi: 10.1016/0003-2697(78)90586-9. [DOI] [PubMed] [Google Scholar]
  14. Nagahashi G., Leonard R. T., Thomson W. W. Purification of plasma membranes from roots of barley: specificity of the phosphotungstic Acid-chromic Acid stain. Plant Physiol. 1978 Jun;61(6):993–999. doi: 10.1104/pp.61.6.993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Nelson N., Deters D. W., Nelson H., Racker E. Partial resolution of the enzymes catalyzing photophosphorylation. 8. Properties of isolated subunits of coupling factor 1 from spinach chloroplasts. J Biol Chem. 1973 Mar 25;248(6):2049–2055. [PubMed] [Google Scholar]
  16. Perlin D. S., Spanswick R. M. Labeling and isolation of plasma membranes from corn leaf protoplasts. Plant Physiol. 1980 Jun;65(6):1053–1057. doi: 10.1104/pp.65.6.1053. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Travis R. L., Booz M. L. Partial Characterization of a Potassium-stimulated Adenosine Triphosphatase from the Plasma Membrane of Meristematic and Mature Soybean Root Tissue. Plant Physiol. 1979 Mar;63(3):573–577. doi: 10.1104/pp.63.3.573. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES