Waechter F, Merdes M, Bieri F, Stäubli W, Bentley P
Eur J Biochem. 1982 Jul;125(2):457-61. doi: 10.1111/j.1432-1033.1982.tb06705.x.
A method for the extensive purification of rabbit liver cytoplasmic epoxide hydrolase is described. The end-product, which was purified 550-fold with respect to the cytosolic fraction, appeared to be more than 85% pure. Results indicate that the enzyme is a dimer of molecular weight 110 000 and consists of two subunits, which are identical or very similar (Mr 57 000) and possess N-terminal serine. Evidence for the existence of aggregates of higher molecular weight was also obtained. The catalytic properties of the cytoplasmic enzyme with styrene oxide as substrate (Km = 3.4 mM; V = 3480 nmol mg-1 min-1) differed markedly from the values published for the microsomal hydrolase.
本文描述了一种用于大规模纯化兔肝胞质环氧化物水解酶的方法。最终产物相对于胞质部分纯化了550倍，纯度似乎超过85%。结果表明，该酶是一种分子量为110000的二聚体，由两个亚基组成，这两个亚基相同或非常相似（Mr 57000），并具有N端丝氨酸。还获得了高分子量聚集体存在的证据。以氧化苯乙烯为底物时，胞质酶的催化特性（Km = 3.4 mM；V = 3480 nmol mg-1 min-1）与已发表的微粒体水解酶的值明显不同。
