Schneckenburger P, Shaw L, Schauer R
Biochemisches Institut, Christian-Albrechts-Universität zu Kiel, FRG.
Glycoconj J. 1994 Jun;11(3):194-203. doi: 10.1007/BF00731218.
CMP-N-acetylneuraminate hydroxylase was isolated from mouse liver high speed supernatant with a yield of 0.4% and an apparent 1000-fold purification. The enzyme is a monomeric protein with a molecular weight of 66 kDa, as determined by gel filtration and SDS-PAGE. The hydroxylase system was reconstituted with Triton X-100-solubilized mouse liver microsomes and purified soluble or microsomal forms of cytochrome b5 reductase and cytochrome b5. The systems were characterized in detail and kinetic parameters for each system were determined.
CMP-N-乙酰神经氨酸羟化酶从小鼠肝脏高速上清液中分离得到，产率为0.4%，表观纯化了1000倍。通过凝胶过滤和SDS-PAGE测定，该酶是一种分子量为66 kDa的单体蛋白。用Triton X-100增溶的小鼠肝脏微粒体以及纯化的可溶性或微粒体形式的细胞色素b5还原酶和细胞色素b5重建羟化酶系统。对这些系统进行了详细表征，并测定了每个系统的动力学参数。
