Alhadeff J A, Andrews-Smith G L
Biochem J. 1979 Feb 1;177(2):753-6. doi: 10.1042/bj1770753.
The subunit composition of human liver alpha-L-fucosidase was studied by using three different procedures for treating and electrophoresing the purified enzyme. Although the presence on only one subunit was found by conventional procedures using sodium dodecyl sulphate and urea, two non-identical subunits with mol. wts. of 59 000 and 54 000 were found when the alpha-L-fucosidase was reduced and S-carboxymethylated with iodoacetate followed by electrophoresis on polyacrylamide gels containing 0.1% sodium dodecyl sulphate and 8.0 M-urea.
通过使用三种不同的方法处理纯化的酶并进行电泳,研究了人肝α-L-岩藻糖苷酶的亚基组成。尽管使用十二烷基硫酸钠和尿素的传统方法仅发现了一个亚基,但当α-L-岩藻糖苷酶用碘乙酸进行还原和S-羧甲基化,然后在含有0.1%十二烷基硫酸钠和8.0M尿素的聚丙烯酰胺凝胶上进行电泳时,发现了两个分子量分别为59000和54000的不同亚基。