PMID: 6109005Nov 1, 1980Paper

Studies on a molecular basis for the heparin-induced regulation of enzymatic activity of mouse striatal tyrosine hydroxylase in vitro. Inhibition of heparin activation and of the enzyme by poly-L-lysyltyrosine and poly-L-lysylphenylalanine and their constituent peptides

Journal of Neurochemistry
A L Stone

Abstract

Tyrosine hydroxylase was purified up to 10-fold from hypotonic extracts of mouse striatum by heparin affinity chromatography. The purified enzyme (a) had a low Km for tyrosine (around 15 microM) and was not inhibited by tyrosine at concentrations up to 0.2 mM when tetrahydrobiopterin was cofactor and (b) was activated by heparin. The interaction of heparin with tyrosine hydroxylase was studied in ways relating to the known interaction with antithrombin. Heparin and keratan sulfates failed to activate tyrosine hydroxylase in place of heparin; several fractions of the bulk heparin (constituting 5 and 15%) had enriched tyrosine hydroxylase-activating potency; and two lysine copolypeptides ((polylysyltyrosine and polylysylphenylalanine) inhibited the activation of tyrosine hydroxylase by heparin. The lysine copolymers also directly inhibited the enzyme. Heparin (but not heparan and keratan sulfates) protected tyrosine hydroxylase from this inhibition. The constituent lysyltyrosyl (but not lysylphenylalanyl) peptide inhibited tyrosine hydroxylase, and heparin also reversed this inhibition, which was sigmoidal (IC50 of 490 microM) and partially competitive with tyrosine. Tyrosine hydroxylase was purified up to sevenfold by lysyltyros...Continue Reading

References

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Jan 1, 1978·Annual Review of Pharmacology and Toxicology·A J Mandell
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Citations

Sep 1, 1993·Protein Science : a Publication of the Protein Society·S C DaubnerP F Fitzpatrick
Jan 1, 1986·Neurochemistry International·A TogariT Nagatsu
May 1, 1986·Journal of Advanced Nursing·D C Jones, G M van Amelsvoort Jones
Nov 13, 1987·Biochemical and Biophysical Research Communications·K KiuchiT Nagatsu

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