Kriegel T, Huse K, Kopperschläger G
Institute of Biochemistry, Karl Marx University Leipzig, GDR.
Biomed Biochim Acta. 1988;47(7):705-11.
The subunits alpha and beta of yeast phosphofructokinase have been separated under denaturing conditions by ion exchange chromatography and then separately immobilized on Sepharose 6MB. The resulting affinity gels were used to fractionate polyclonal phosphofructokinase antisera from rabbit into subunit-specific antibodies. In addition to subunit-specific antibodies also antibody fractions which recognize both types of subunits of phosphofructokinase could be desorbed from the affinity gels. Antibodies directed either to the alpha- or to the beta-subunits were found to inhibit the enzyme activity. The results are discussed in terms of a partial identity of the alpha- and beta-chain of phosphofructokinase.
酵母磷酸果糖激酶的α和β亚基在变性条件下通过离子交换色谱法分离，然后分别固定在琼脂糖6MB上。所得的亲和凝胶用于将兔的多克隆磷酸果糖激酶抗血清分离成亚基特异性抗体。除了亚基特异性抗体外，还可以从亲和凝胶上解吸出识别磷酸果糖激酶两种亚基的抗体组分。发现针对α亚基或β亚基的抗体均能抑制酶活性。根据磷酸果糖激酶α链和β链的部分同一性对结果进行了讨论。
