Ichinose H, Kojima K, Togari A, Kato Y, Parvez S, Parvez H, Nagatsu T
Anal Biochem. 1985 Nov 1;150(2):408-14. doi: 10.1016/0003-2697(85)90529-9.
We purified aromatic L-amino acid decarboxylase (AADC) homogeneously and rapidly from human pheochromocytoma using high-performance liquid chromatography. HPLC with gel permeation and hydrophobic columns was highly effective, and the entire purification could be finished within 3 days. Purified AADC showed a single band with an Mr of 50,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and decarboxylated L-3,4-dihydroxyphenylalanine, L-5-hydroxytryptophan, and L-threo-3,4-dihydroxyphenylserine (a synthetic precursor of natural norepinephrine). Amino acid analysis of purified AADC was performed.
我们使用高效液相色谱法从人嗜铬细胞瘤中快速纯化出了均一的芳香族L-氨基酸脱羧酶（AADC）。带有凝胶渗透柱和疏水柱的高效液相色谱法非常有效，整个纯化过程可在3天内完成。纯化后的AADC在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上显示出一条分子量为50,000的条带，并且能使L-3,4-二羟基苯丙氨酸、L-5-羟色氨酸和L-苏式-3,4-二羟基苯丝氨酸（天然去甲肾上腺素的合成前体）脱羧。对纯化后的AADC进行了氨基酸分析。
