Schmidt K H, Klessen C, Köhler W, Malke H
Institute of Microbiology and Experimental Therapy, Jena, F.R.G.
J Immunol Methods. 1991 Sep 20;143(1):111-7. doi: 10.1016/0022-1759(91)90279-o.
The streptococcal streptokinase gene truncated at its 5' end was fused to regions of the staphylococcal protein A gene encoding the Fc-binding domains A and B. The resultant fusion gene, when expressed in the Escherichia coli lacPO system or under the speA expression/secretion signals in S. sanguis, specified a bifunctional hybrid protein, SPA-SKC, capable of Fc binding and plasminogen activation. When used in immunoassays designed to titrate antisera raised against bovine chymosin, human serum albumin and fibrinogen, the assay using SPA-SKC compared well with that using a commercial SPA-enzyme conjugate. The simple preparative method together with its efficacy and ease of use, make SPA-SKC a potentially valuable detector reagent in quantitative immunology.
在其5'端截短的链球菌链激酶基因与编码Fc结合结构域A和B的葡萄球菌蛋白A基因区域融合。所得融合基因在大肠杆菌lacPO系统中表达时，或在血链球菌的speA表达/分泌信号下表达时，产生一种双功能杂合蛋白SPA-SKC，它能够结合Fc并激活纤溶酶原。当用于旨在滴定针对牛凝乳酶、人血清白蛋白和纤维蛋白原产生的抗血清的免疫测定时，使用SPA-SKC的测定与使用商业SPA-酶偶联物的测定效果相当。这种简单的制备方法及其有效性和易用性，使SPA-SKC成为定量免疫学中一种潜在有价值的检测试剂。
