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Brauer D, Nungesser E, Maxwell RJ, et al. Evidence for and subcellular localization of a ca-stimulated phospholipase d from maize roots. Plant Physiol. 1990;92(3):672-8doi: 10.1104/pp.92.3.672.
Brauer, D., Nungesser, E., Maxwell, R. J., Schubert, C., & Tu, S. L. (1990). Evidence for and subcellular localization of a ca-stimulated phospholipase d from maize roots. Plant physiology, 92(3), 672-8. https://doi.org/10.1104/pp.92.3.672
Brauer, D, et al. "Evidence for and subcellular localization of a ca-stimulated phospholipase d from maize roots." Plant physiology vol. 92,3 (1990): 672-8. doi: https://doi.org/10.1104/pp.92.3.672
Brauer D, Nungesser E, Maxwell RJ, Schubert C, Tu SL. Evidence for and subcellular localization of a ca-stimulated phospholipase d from maize roots. Plant Physiol. 1990 Mar;92(3):672-8. doi: 10.1104/pp.92.3.672. PMID: 16667333; PMCID: PMC1062352.
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Plant Physiol. 1990 Mar;92(3):672-8. doi: 10.1104/pp.92.3.672.

Evidence for and subcellular localization of a ca-stimulated phospholipase d from maize roots.

Plant physiology

D Brauer, E Nungesser, R J Maxwell, C Schubert, S L Tu

Affiliations

  1. Plant and Soil Biophysics Research Unit, Eastern Regional Research Center, Agricultural Research Service, Philadelphia, Pennsylvania 19118.

PMID: 16667333 PMCID: PMC1062352 DOI: 10.1104/pp.92.3.672

Abstract

Autolytic lipid changes in corn (Zea mays L.) root crude homogenates and isolated membranes were examined by the use of high performance thin-layer chromatography. In the absence of added CaCl(2), losses in phosphatidylcholine and other phospholipids corresponds to increase in fatty acids without the accumulation of either phosphatidic acid or lyso-phosphatidylcholine. However, in the presence of 1 millimolar CaCl(2), phosphatidylcholine concentrations declined more rapidly with an immediate increase in phoshatidic acid, and slower rate of fatty acid accumulation. Autolytic phospholipid degradation yielded primarily free fatty acids in the absence of Ca and phosphatidic acid in the presence of 1 millimolar CaCl(2), suggesting the presence of an acyl hydrolase and phospholipase D activities. Differential centrifugation studies indicate that 50 to 80% of the crude homogenate's phospholipase D activity is membrane-bound. Density centrifugation experiments suggest that the membrane-bound phospholipase D activity is localized primarily on mitochondrial membranes.

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