Dephosphorylation of purified brain tyrosine hydroxylase by rat striatal extracts.
作者： Mitchell A. Lazar , Joachim D. Raese , Jack D. Barchas
DOI: 10.1016/0197-0186(83)90016-5
关键词:
摘要: Tyrosine hydroxylase (TH) was purified from bovine brain and enzymatically phosphorylated in vitro. Radioactively TH dephosphorylated by rat tissue extracts. Of tissues examined, corpus striatal extracts were highest specific activity the dephosphorylating assay. Phosphorylated histone did not inhibit dephosphorylation of The thermal decay varied with substrate, most unstable activities assayed. results suggest that can be that, striatum, this process differs quantitatively phosphohistone phosphoprotamine.
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