In vitro translation of human pheochromocytoma messenger RNAs: characterization of tyrosine-hydroxylase and dopamine-beta-hydroxylase.
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.
Benlot
C
C
Antreassian
J
J
Henry
J P
JP
Legrand
J C
JC
Gros
F
F
Thibault
J
J
D000310:Adrenal Gland Neoplasms / Q000201:enzymology*; D002474:Cell-Free System; D002499:Centrifugation, Density Gradient; D004299:Dopamine beta-Hydroxylase / Q000096:biosynthesis* / Q000235:genetics; D004792:Enzyme Precursors / Q000096:biosynthesis*; D006801:Humans; D007163:Immunosorbent Techniques; D008970:Molecular Weight; D010673:Pheochromocytoma / Q000201:enzymology*; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D014446:Tyrosine 3-Monooxygenase / Q000235:genetics
D004792:Enzyme Precursors; D012333:RNA, Messenger; D014446:Tyrosine 3-Monooxygenase; D004299:Dopamine beta-Hydroxylase