Dephosphorylation of purified brain tyrosine hydroxylase by rat striatal extracts.

Abstract:

:Tyrosine hydroxylase (TH) was purified from bovine brain and enzymatically phosphorylated in vitro. Radioactively phosphorylated TH was dephosphorylated by rat tissue extracts. Of tissues examined, rat corpus striatal extracts were highest in specific activity in the TH dephosphorylating assay. Phosphorylated histone did not inhibit dephosphorylation of TH by rat striatal extracts. The thermal decay of dephosphorylating activity of rat striatal extracts varied with substrate, with TH dephosphorylating activity most unstable of the activities assayed. The results suggest that TH can be enzymatically dephosphorylated and that, in corpus striatum, this process differs quantitatively from the dephosphorylation of phosphohistone and phosphoprotamine.

journal_name

Neurochem Int

authors

Lazar MA,Raese JD,Barchas JD

doi

10.1016/0197-0186(83)90016-5

subject

Has Abstract

pub_date

1983-01-01 00:00:00

pages

107-11

issue

1

eissn

0197-0186

issn

1872-9754

pii

0197-0186(83)90016-5

journal_volume

5

pub_type

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