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 Intjournal_title
Neurochemistry internationalauthors
Lazar MA,Raese JD,Barchas JDdoi
10.1016/0197-0186(83)90016-5subject
Has Abstractpub_date
1983-01-01 00:00:00pages
107-11issue
1eissn
0197-0186issn
1872-9754pii
0197-0186(83)90016-5journal_volume
5pub_type
杂志文章abstract::Bindings of glutamate receptor agonists and related modulators were investigated in 10 discrete tissues from gerbil brain using a biochemical technique. There appeared considerable discrepancies, in respect of intrahippocampal profiles, from reported data by autoradiography on rat brain. In the gerbil, an almost equiv...
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journal_title:Neurochemistry international
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journal_title:Neurochemistry international
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