Abstract
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.
Publication types
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Comparative Study
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English Abstract
MeSH terms
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Adrenal Gland Neoplasms / enzymology*
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Amino Acid Sequence
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Animals
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Aromatic-L-Amino-Acid Decarboxylases / isolation & purification*
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Chromatography, High Pressure Liquid
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Dopa Decarboxylase / analysis
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Dopa Decarboxylase / isolation & purification*
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Electrophoresis, Polyacrylamide Gel
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Molecular Sequence Data
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Pheochromocytoma / enzymology*
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Rats
Substances
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Dopa Decarboxylase
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Aromatic-L-Amino-Acid Decarboxylases