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Utilization of a Monoclonal Antibody to Study in Vitro Phosphorylation of a Low Km Phosphodiesterase

  • David H. Reifsnyder
  • Scott A. Harrison
  • Colin H. Macphee
  • Joseph A. Beavo
Conference paper
Part of the NATO ASI Series book series (NSSA, volume 135)

Abstract

The study of cyclic nucleotide phosphodiesterases in tissues is complicated by the presence of isozymes that differ in terms of selective substrate specificity, substrate affinity, and regulatory and physical properties (for review see Beavo et al., 1982 or Wells and Hardman, 1977). Because the phosphodiesterase isozymes are trace cellular proteins which require several thousand-fold purification to apparent homogeneity, the isolation of these isozymes is very difficult. Isozyme specific probes are needed to study the enzymes in crude systems.

Keywords

Dependent Protein Kinase Bovine Heart Phosphodiesterase Activity Cyclic Nucleotide Phosphodiesterase cAMP Phosphodiesterase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • David H. Reifsnyder
    • 1
  • Scott A. Harrison
    • 1
  • Colin H. Macphee
    • 1
  • Joseph A. Beavo
    • 1
  1. 1.Department of Pharmacology, SJ-30University of WashingtonSeattleUSA

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