Goueli S A, Davis A T, Arfman E, Vessella R, Ahmed K
Department of Laboratory Medicine and Pathology, University of Minnesota School of Medicine, Minneapolis.
Hybridoma. 1990 Dec;9(6):609-18. doi: 10.1089/hyb.1990.9.609.
A monoclonal antibody was produced against the nuclear casein kinase II (PK-N2) isolated from rat liver. The antibody was of the IgM class, and showed immunoreactivity towards the higher molecular weight subunit (41K Da) of the protein kinase in Western blots. The antibody was equally reactive towards the PK-N2 isolated from rat ventral prostate indicating that it can recognize the enzyme from different tissues of the rat. The antibody also detected the cytosolic casein kinase II (CK-2) suggesting significant similarity of the antigenic domains in the two forms of this protein kinase. No binding was detected with the nuclear or cytosolic casein kinase I (PK-N1 and CK-1). The antibody did not inhibit the enzyme activity or directly precipitate the enzyme, but when coupled to an affinity matrix and cross-linked with dimethylpimelimidate, it was capable of removing nearly all the PK-N2 activity from solution.
制备了一种针对从大鼠肝脏分离出的核酪蛋白激酶II(PK-N2)的单克隆抗体。该抗体为IgM类,在蛋白质印迹中对蛋白激酶的高分子量亚基(41K Da)显示出免疫反应性。该抗体对从大鼠腹侧前列腺分离出的PK-N2具有同等反应性,表明它可以识别大鼠不同组织中的该酶。该抗体还检测到胞质酪蛋白激酶II(CK-2),表明这种蛋白激酶的两种形式中抗原结构域具有显著相似性。未检测到与核或胞质酪蛋白激酶I(PK-N1和CK-1)的结合。该抗体不抑制酶活性或直接沉淀酶,但当与亲和基质偶联并与二甲基哌嗪二亚胺交联时,它能够从溶液中去除几乎所有的PK-N2活性。