[Purification and partial sequencing of L-dopa decarboxylase from pheochromocytoma in rats].
L-DOPA decarboxylase was purified from rat pheochromocytoma. Tryptic digestion of this enzyme permitted obtaining fourteen peptides. The comparison of the sequence of L-DOPA decarboxylase from other species with one of these peptides demonstrates a great preservation of this protein.
Cogé
F
F
Laboratoire de Biochimie cellulaire, Collège de France, Paris.
Krieger-Poullet
M
M
Guillemot
J C
JC
Ferrara
P
P
Gros
F
F
Thibault
J
J
D000310:Adrenal Gland Neoplasms / Q000201:enzymology*; D000595:Amino Acid Sequence; D000818:Animals; D001142:Aromatic-L-Amino-Acid Decarboxylases / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid; D004296:Dopa Decarboxylase / Q000032:analysis / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010673:Pheochromocytoma / Q000201:enzymology*; D051381:Rats
D004296:Dopa Decarboxylase; D001142:Aromatic-L-Amino-Acid Decarboxylases
Purification et séquençage partiel de la L-dopa décarboxylase de phéochromocytome de rat.