通过亲和层析纯化的猪脑磷酸果糖激酶中两种活性组分的分离与鉴定。

Isolation and characterization of the two active fractions from porcine brain phosphofructokinase purified by affinity chromatography.

作者信息

Hachimori A, Maekawa N, Iizuka E

出版信息

Comp Biochem Physiol B. 1986;85(1):105-11. doi: 10.1016/0305-0491(86)90229-4.

Abstract

Phosphofructokinase was purified from porcine brain by the successive affinity chromatographies of Blue-Sepharose and ATP-agarose. The purified enzyme was found to contain three subunits, namely, the L-, M- and C-type by SDS-polyacrylamide gel electrophoresis (SDS-PAGE). The purified enzyme separated into the two active fractions through gel filtration (FIs and FIIs). SDS-PAGE revealed that the FIs contained the L- and M-type subunits, while the FIIs contained the M- and C-type. The FIIs preparation was more sensitive to ATP inhibition, ADP activation and citrate inhibition than the FIs.

摘要

通过Blue-Sepharose和ATP-琼脂糖的连续亲和层析从猪脑中纯化磷酸果糖激酶。通过SDS-聚丙烯酰胺凝胶电泳（SDS-PAGE）发现纯化的酶含有三个亚基，即L型、M型和C型。通过凝胶过滤将纯化的酶分离成两个活性部分（FIs和FIIs）。SDS-PAGE显示FIs含有L型和M型亚基，而FIIs含有M型和C型。FIIs制剂比FIs对ATP抑制、ADP激活和柠檬酸抑制更敏感。