Srinivasan K, Awapara J
Biochim Biophys Acta. 1978 Oct 12;526(2):597-604. doi: 10.1016/0005-2744(78)90150-x.
DOPA decarboxylase (aromatic-l-amino-acid carboxy-lyase, EC 4.1.1.28) from guinea pig kidneys has been purified to a specific activity of 9370 or 330-fold. Efficient purification was possible by employing apolar interaction chromatography. The purified enzyme gives a single component on polyacrylamide gel electrophoresis and the absorption spectrum of the enzyme reveals two forms of binding of pyridoxal 5-phosphate. The pure enzyme decarboxylates l-DOPA, 5-hydroxytryptophan, o-tyrosine and m-tyrosine but it is inactive towards phenylalanine, tyrosine, tryptophan, histidine and 3-methoxy-phenylalanine. The enzyme behaves as an undissociated enzyme but only towards 5-hydroxytryptophan. It behaves as an enzyme from which the coenzyme is partially dissociated when it attacks l-DOPA, o-tyrosine and m-tyrosine.
豚鼠肾脏中的多巴脱羧酶（芳香族L-氨基酸羧基裂解酶，EC 4.1.1.28）已被纯化至比活性为9370，即纯化了330倍。采用非极性相互作用色谱法可实现高效纯化。纯化后的酶在聚丙烯酰胺凝胶电泳上呈现单一成分，且该酶的吸收光谱显示磷酸吡哆醛存在两种结合形式。纯酶可使L-多巴、5-羟色氨酸、邻酪氨酸和间酪氨酸脱羧，但对苯丙氨酸、酪氨酸、色氨酸、组氨酸和3-甲氧基苯丙氨酸无活性。该酶表现为一种未解离的酶，但仅对5-羟色氨酸如此。当它作用于L-多巴、邻酪氨酸和间酪氨酸时，表现为一种辅酶部分解离的酶。
