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Calcium-Independent Activation of Protein Kinase C by the Dianionic Form of Phosphatidic Acid

Authors
Publisher
Elsevier Inc.
Publication Date
Volume
190
Issue
1
Identifiers
DOI: 10.1006/bbrc.1993.1006
Disciplines
  • Biology

Abstract

Abstract Phosphatidic acid in the form of small unilamellar vesicles has a dissociation constant of about 8.3 as determined by 31P nuclear magnetic resonance (NMR) spectroscopy. The activation of protein kinase C (PKC) by monovalent phosphatidic acid or phosphatidylserine occurs only in the presence of Ca 2+. However, PKC activity on membranes of divalent anionic phosphatidic acid is independent of Ca 2+ concentration.

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