Chemistry of Natural Compounds

, Volume 30, Issue 1, pp 92–96 | Cite as

A Ca2+-phospholipid-dependent protein kinase from cottonplant shoots

  • Zh. A. Abdurakhmanova
  • L. N. Abdusalyamova
  • V. V. Kim
  • Sh. I. Salikhov


The Ca2+-phospholipid-dependent protein kinase from cottonplant shoots was purified by chromatography on DEAE-Sepharose CL-6B, and then on phenyl-Sepharose CL-4B. According to electrophoresis in PAAG, the enzyme was practically homogeneous and had a molecular mass of ∼ 57 kDa. In the presence of Ca2+ alone, the enzyme was activated to only a slight degree. Under the combined action of Ca2+ and a phospholipid the action of the enzyme rose severalfold. A determination of amino acid specificity showed that the protein kinase isolated was a serine- and threonine-specific protein kinase.


Protein Kinase Organic Chemistry Serine Molecular Mass Combine Action 
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Copyright information

© Plenum Publishing Corporation 1994

Authors and Affiliations

  • Zh. A. Abdurakhmanova
  • L. N. Abdusalyamova
  • V. V. Kim
  • Sh. I. Salikhov

There are no affiliations available

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