Macartney H W, Tschesche H
Hoppe Seylers Z Physiol Chem. 1981 Nov;362(11):1523-31. doi: 10.1515/bchm2.1981.362.2.1523.
Latent human PMN leucocyte collagenase (enzyme-inhibitor complex) was shown to require zinc for the property of being activatable by various disulfides [see Macartney, H.W. and Tschesche, H. (1980) FEBS Lett. 119, 327--332]. The active enzyme also requires zinc for activity, indicating a possible participation in the enzyme's reaction mechanism and/or stabilization of the active site. The zinc in the latent enzyme may be removed by dialysis against EDTA, or cysteine. This produces a zinc-free latent enzyme which cannot be activated by any of the disulfide-containing activators. Readdition of zinc to the EDTA-inhibited latent enzyme, at the same concentration as the EDTA, produces an activatable latent enzyme once again. However, excessive zinc concentrations (more than three times the concentration of EDTA) exhibited an inhibitory effect on the activation process. Thereafter the inhibitor cannot be removed by disulfides from the enzyme-inhibitor complex of the latent enzyme. The zinc in the latent enzyme may be replaced by other double-positive metal ions such as cobalt, manganese, magnesium and copper.
潜在的人中性粒细胞胶原酶（酶 - 抑制剂复合物）已被证明需要锌才能被各种二硫化物激活[见Macartney, H.W.和Tschesche, H.（1980年）《欧洲生物化学学会联合会快报》119, 327 - 332]。活性酶也需要锌来发挥活性，这表明锌可能参与了酶的反应机制和/或活性位点的稳定。潜在酶中的锌可以通过用EDTA或半胱氨酸透析去除。这会产生一种无锌的潜在酶，它不能被任何含二硫化物的激活剂激活。以与EDTA相同的浓度向EDTA抑制的潜在酶中重新添加锌，会再次产生可激活的潜在酶。然而，过高的锌浓度（超过EDTA浓度的三倍）对激活过程表现出抑制作用。此后，抑制剂不能从潜在酶的酶 - 抑制剂复合物中被二硫化物去除。潜在酶中的锌可以被其他双价金属离子如钴、锰、镁和铜取代。
