酶是生物催化剂，在数以千计的酶中，第一大类以烟酰胺腺嘌呤核苷酸（ＮＡＤ／ＮＡＤＨ）为辅酶的多种氧化－还原酶需要金属离子作为辅助因子而发生独特的催化功能。其中含锌的醇脱氨酶（ＡＤＨ）是目前研究得最多的一种。本文用电化学分析法研究稀土离子对乳酸脱氢酶（ＬＤＨ）和谷氨酸脱氢酶（ＧＤＨ）两体系的作用时也探讨了Ｚｎ２＋在此两体系中的作用。结果指出在ＬＤＨ体系中不需要 Ｚｎ２＋；在 ＧＤＨ（牛肝中提取）体系中， Ｚｎ２＋是一种强抑制剂，Ｅｕ３＋可以缓解它的抑制作用，但是在黄瓜根系提取的粗ＧＤＨ体系中，Ｚｎ２＋必需存在于反介质中起激活酶的催化作用。 Enzymes are biocatalysts and among the thousands of enzymes, the first major class of various oxidoreductases that use nicotinamide adenine nucleotides (NAD / NADH) as coenzymes requires unique metal ions as cofactors Catalytic function. One zinc-containing alcohol deaminase (ADH) is currently the most studied one. In this paper, the electrochemical analysis of rare earth ions on lactate dehydrogenase (LDH) and glutamate dehydrogenase (GDH) of the two systems also explored the role of Zn2 + in these two systems. The results showed that Zn2 + was not required in LDH system; Zn2 + was a potent inhibitor in GDH (extract from bovine liver), and Eu3 + could alleviate its inhibitory effect. However, in the crude GDH system extracted from cucumber roots, Zn2 + Exist in the anti-media to activate the catalytic role of enzymes.