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In vitro translation of human pheochromocytoma messenger RNAs: characterization of tyrosine-hydroxylase and dopamine-beta-hydroxylase
Authors:C Benlot  J Antreassian  J P Henry  J C Legrand  F Gros  J Thibault
Abstract:mRNAs extracted from human pheochromocytoma were translated in vitro in a lysate of a rabbit reticulocytes. Two enzymes of the biosynthetic pathway of the catecholamines, tyrosine-hydroxylase (TH) and dopamine-beta-hydroxylase (DBH), were characterized as translation products after immunoprecipitation by specific antisera and electrophoretic analysis. The precursor of TH is a polypeptide having a molecular mass of 62,000 identical to that found for the mature protein. The molecular mass of the precursor of DBH 73,000 while that of the mature form is 79,000. TH and DBH have been translated from mRNAs having sedimentation coefficients of 22S and 25S, respectively.
Keywords:tyrosine-hydroxylase  dopamine-β-hydroxylase  pheochromocytome humain  in vitro translation  tyrosine-hydroxylase  dopamine-β-hydroxylase  human pheochromocytoma  TH  Tyrosine hydroxylase  DDC  DOPA decarboxylase  DBH  Dopamine beta hydroxylase  PNMT  Phenylethanolamine-N-méthyl transferase  SDS  Sodium dodecyl sulfate  Mr  Molecular mass  Polyadenylated RNA
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