Bloemendal H, Jansen K
Department of Biochemistry, University of Nijmegen, The Netherlands.
Biochim Biophys Acta. 1988 Jul 14;966(1):117-21. doi: 10.1016/0304-4165(88)90135-3.
Human placental alkaline RNAase inhibitor was purified to homogeneity. Activity was measured after each purification step. The final identification of the purified protein was done by two-dimensional polyacrylamide gel electrophoresis and by immunoblotting. Antibodies were prepared by immunization of rabbits with the highly purified inhibitor. The availability of the antiserum directed against the human inhibitor enabled the detection of RNAase inhibitor from various other organs and species. This procedure has the advantage over the usual activity test in that the inhibitor can be found even if its activity has been lost.
人胎盘碱性RNA酶抑制剂被纯化至同质状态。在每一步纯化后测量活性。通过二维聚丙烯酰胺凝胶电泳和免疫印迹对纯化后的蛋白质进行最终鉴定。用高度纯化的抑制剂免疫兔子制备抗体。针对人抑制剂的抗血清的可用性使得能够从各种其他器官和物种中检测RNA酶抑制剂。该方法相对于常规活性测试具有优势，因为即使抑制剂的活性已经丧失也能检测到它。
