Rahman M K, Togari A, Kojima K, Takahashi K, Nagatsu T
Mol Cell Biochem. 1984 Aug;63(1):53-8. doi: 10.1007/BF00230161.
In the course of our studies on the developmental changes of aromatic L-amino acid decarboxylase (AADC) in the serum of Japanese monkeys (Macaca fuscata fuscata), we found the presence of an endogenous inhibitor of AADC in all stages of monkey life. This inhibitor inhibited the serum enzyme activity completely with L-5-hydroxytryptophan (L-5-HTP) as substrate, while the activity was partially inhibited with L-DOPA as substrate. The inhibitor was non-dialyzable, but it could be removed from the monkey serum by DEAE-Sephacel chromatography. After this treatment AADC activities could be detected in the monkey serum by using both L-DOPA and L-5-HTP as substrates. Moreover, the total activity for L-DOPA was augmented by 3-fold in the serum after the removal of the inhibitor. Serum AADC was partially purified from monkey and compared with that of rat using both L-DOPA and L-5-HTP as substrates, but the ratio of the activities for the two substrates did not change significantly in each fraction during purification from either monkey or rat serum.
在我们对日本猕猴（食蟹猕猴指名亚种）血清中芳香族L-氨基酸脱羧酶（AADC）发育变化的研究过程中，我们发现在猕猴生命的各个阶段都存在一种AADC的内源性抑制剂。该抑制剂以L-5-羟色氨酸（L-5-HTP）为底物时能完全抑制血清酶活性，而以L-多巴为底物时活性受到部分抑制。该抑制剂不能透析，但可通过DEAE-葡聚糖凝胶柱色谱法从猕猴血清中去除。经过这种处理后，以L-多巴和L-5-HTP为底物时均可在猕猴血清中检测到AADC活性。此外，去除抑制剂后血清中L-多巴的总活性增加了3倍。从猕猴血清中对血清AADC进行了部分纯化，并以L-多巴和L-5-HTP为底物与大鼠的血清AADC进行比较，但在从猕猴或大鼠血清中纯化的每个组分中，两种底物的活性比值均未发生显著变化。
