Yuan X H, Kwiatkowska D, Kemp R G
Department of Biological Chemistry and Structure, University of Health Sciences, Chicago Medical School, Illinois 60065.
Biochem Biophys Res Commun. 1988 Jul 15;154(1):113-7. doi: 10.1016/0006-291x(88)90657-2.
A procedure was developed for the purification of inorganic pyrophosphate: fructose-6-phosphate 1-phospho-transferase (PPi-PFK) from potato tubers. The enzyme has the structure alpha 4 beta 4 with a subunit of 68 kDa and a beta subunit of 60 kDa. The structural relationship of this enzyme to other PFKs and to fructose bisphosphatase was examined by immunoprecipitation and immunoblotting. Antibodies to the plant enzyme did not react with E. coli PFK. No cross-reaction was seen among the following enzymes or their antibodies: yeast fructose bisphosphatase; rabbit PFKs A, B, or the enzyme from brain; and the two subunits of the potato PPi-PFK. On the other hand, antibody to E. coli PFK-1 strongly cross-reacts with the 60 kDa polypeptide but not 68 kDa peptide.
果糖-6-磷酸1-磷酸转移酶（PPi-PFK）的方法。该酶具有α4β4结构，α亚基为68 kDa，β亚基为60 kDa。通过免疫沉淀和免疫印迹研究了这种酶与其他磷酸果糖激酶（PFK）以及果糖双磷酸酶之间的结构关系。针对该植物酶的抗体与大肠杆菌PFK不发生反应。在以下酶或其抗体之间未观察到交叉反应：酵母果糖双磷酸酶；兔PFK A、B或来自脑的酶；以及马铃薯PPi-PFK的两个亚基。另一方面，针对大肠杆菌PFK-1的抗体与60 kDa多肽强烈交叉反应，但与68 kDa肽不发生交叉反应。
