Berti A, Stefani M, Camici G, Manao G, Cappugi G, Degl'Innocenti D, Ramponi G
Int J Pept Protein Res. 1986 Jul;28(1):15-21. doi: 10.1111/j.1399-3011.1986.tb03225.x.
Modifications in the muscle acylphosphatase purification procedure enabled us to isolate the enzyme with its sole cysteine in the -SH form; this enzyme form is the most abundant in vivo. Our data demonstrates that the enzyme forms purified by previously reported procedures can be easily derived from a reaction of the SH-enzyme with oxidized glutathione. Probably most, or even all, of these enzyme forms are artifacts due to the purification. The SH-acylphosphatase shows kinetic parameters similar to those reported for the mixed disulfide with glutathione and S-S dimer, except for the specific activity value, which is about twice as much, and the Km, which is reduced.
肌肉酰基磷酸酶纯化程序的改进使我们能够分离出其唯一的半胱氨酸以-SH形式存在的酶；这种酶形式在体内最为丰富。我们的数据表明，通过先前报道的程序纯化的酶形式很容易由SH-酶与氧化型谷胱甘肽的反应产生。可能这些酶形式中的大多数甚至全部都是纯化过程中产生的假象。SH-酰基磷酸酶的动力学参数与报道的与谷胱甘肽的混合二硫键和S-S二聚体的动力学参数相似，只是比活性值约高两倍，而Km值降低。
