Chevalier M, de Gunzburg J, Veron M
Biochem Biophys Res Commun. 1986 Apr 29;136(2):651-6. doi: 10.1016/0006-291x(86)90490-0.
The purified regulatory (R) and catalytic (C) subunits of cAMP dependent protein kinase (cAK) from the primitive eukaryote Dictyostelium discoideum have been compared with the homologous proteins from bovine heart by SDS-PAGE followed by Western blotting using polyclonal antibodies. No cross-reaction could be demonstrated by this technique although the slime mold subunits share several functional properties with their mammalian counterparts and are able to form functional hybrid holoenzymes.
通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE),随后使用多克隆抗体进行蛋白质免疫印迹法,对来自原始真核生物盘基网柄菌的环磷酸腺苷依赖性蛋白激酶(cAK)的纯化调节(R)亚基和催化(C)亚基,与来自牛心脏的同源蛋白进行了比较。尽管黏菌亚基与其哺乳动物对应物具有若干功能特性,并且能够形成功能性杂交全酶,但通过该技术未显示出交叉反应。