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Related Experiment Videos

Adenosine triphosphatase from soybean callus and root cells.

D L Hendrix1, R M Kennedy

  • 1Department of Biology, University of Houston, Houston, Texas 77004.

Plant Physiology
|February 1, 1977
PubMed
Summary

Soybean root and callus plasma membranes contain ATPase enzymes. These enzymes are activated by specific divalent and monovalent ions, with optimal activity at pH 6.5 and preferring ATP as a substrate.

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Area of Science:

  • Plant Cell Biology
  • Biochemistry
  • Membrane Transport

Background:

  • Plasma membrane-bound ATPases are crucial for cellular functions in plants.
  • Understanding the specific characteristics of these enzymes aids in elucidating nutrient transport and signaling pathways.

Purpose of the Study:

  • To characterize the ATPase activity in membrane fractions from soybean (Glycine max L.) root and callus cells.
  • To determine ion stimulation, pH optima, and nucleotide specificity of the plasma membrane-associated ATPase.

Main Methods:

  • Isolation and enrichment of a plasma membrane fraction from soybean root and callus cells.
  • Assay of ATPase activity under varying conditions of divalent cations, monovalent salts, and pH.
  • Determination of nucleotide specificity through substrate variation.

Main Results:

  • ATPase activity was stimulated by divalent cations (Mg2+ > Mn2+ > Zn2+ > Ca2+ > Sr2+) and further enhanced by monovalent salts.
  • Root cell preparations showed a preference for K+ over other monovalent ions, while callus preparations slightly preferred Na+.
  • The optimal pH for ATP hydrolysis was 6.5, and the enzyme exhibited a strong preference for ATP over other nucleotides.

Conclusions:

  • The characterized ATPase activity is likely associated with the plasma membrane of soybean root and callus cells.
  • Ion and pH preferences suggest specific roles in cellular ion homeostasis and energy transduction.
  • The enzyme's specificity for ATP highlights its role in active transport processes.

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