A Kinetic Study of Bovine Adrenal Tyrosine Hydroxylase
نویسندگان
چکیده
منابع مشابه
Studies on tyrosine hydroxylase from bovine adrenal medulla.
Approximately 90% of the total tyrosine hydroxylase activity of bovine adrenal medulla homogenates was localized in the particulate fraction of the homogenate. The particulate enzyme was solubilized by incubation with trypsin, and the solubilized enzyme was partially purified. This enzyme was found to behave like the tyrosine hydroxylase which had been purified from the supernatant fraction by ...
متن کاملInhibitors of purified beef adrenal tyrosine hydroxylase.
Two classes of compounds have been investigated as inhibitors of purified beef adrenal tyrosine hydroxylase. Among the aromatic amino acids tyrosine analogues were found to be most potent, particularly those having an a-methyl or 3-halogen substitution. Two normal metabolites, monoand diiodo-tyrosine, were found to bevery effective inhibitors. Inhibition by the amino acid analogues was shown to...
متن کاملInfluence of cell-cell contact on levels of tyrosine hydroxylase in cultured bovine adrenal chromaffin cells.
We have studied the regulation of tyrosine hydroxylase by cell-cell contact in primary cultures of bovine adrenal chromaffin cells. Preparation of dissociated chromaffin cells from bovine adrenal medullae or the harvesting of cultured cells resulted in a rapid decrease of the specific mRNA(TH) (defined as the amount of mRNA(TH) (where TH represents tyrosine hydroxylase) per microgram of total R...
متن کاملEffects of phorbol ester on tyrosine hydroxylase phosphorylation and activation in cultured bovine adrenal chromaffin cells.
The phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA) caused phosphorylation of phosphoproteins of 56-kDa which co-migrated with and had identical pI values to subunits of tyrosine hydroxylase. The phosphorylation was closely correlated with an increase of [3H]3,4-dihydroxyphenylalanine (DOPA) production which is a reflection of increased tyrosine hydroxylase activity. Only those phorbol...
متن کاملIn vitro phosphorylation of bovine adrenal tyrosine hydroxylase by adenosine 3':5'-monophosphate-dependent protein kinase.
We have studied the effects of adenosine 3':5'-monophosphate (cAMP)-dependent protein kinase on the phosphorylative and functional modification of bovine adrenal tyrosine hydroxylase. Incubation of partially purified tyrosine hydroxylase with cAMP-dependent protein kinase in the presence of [gamma32P]ATP and 5 micron cAMP led to a 3- to 5-fold activation of tyrosine hydroxylase and to incorpora...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1966
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)99741-3