Mar 11, 1976

Activation of tyrosine hydroxylase by polyanions and salts. An electrostatic effect

Biochimica Et Biophysica Acta
I R KatzS Kaufman

Abstract

The activity of a partially purified preparation of tyrosine hydroxylase (EC 1.14.16.2) from the bovine caudate nucleus was increased by heparin, chondroitin sulfate, phosphatidylserine, polyacrylic acid, polyvinyl sulfuric acid and both poly-D-, and poly-L-glutamic acids, all polyanions. A variety of salts both activated the enzyme and prevented the activation by the polyanions. The observations that activity is increased when the enzyme interacts with salts and with macromolecules of high negative charge density are used to infer a model for these interactions and for the structural change in the enzyme that accompanies activation.

  • References2
  • Citations27

References

Mentioned in this Paper

Heparin
Sulfuric acid
Phosphatidylserines
Polyacrylic Acid
Bos taurus
Liquaemin
Poly D
Polyanion
phosphatidylserine
Macromolecule

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