Garamszegi N, Garamszegi Z P, Rogers M S, DeMarco S J, Strehler E E
Mayo Graduate School, Mayo Clinic/Foundation, Rochester, MN 55905, USA.
Biotechniques. 1997 Nov;23(5):864-6, 868-70, 872. doi: 10.2144/97235st02.
The green fluorescent protein (GFP) of the jellyfish Aequorea victoria is an emerging tool to monitor gene expression in situ and in vivo. Because of its fluorescence properties, when GFP is fused in-frame to a specific protein of interest, various aspects of the behavior of this protein can be analyzed noninvasively. Here we describe a fusion between GFP and human calmodulin-like protein (CLP) and show that this protein retains fluorescence and known characteristics of CLP, including Ca(2+)-dependent interaction with phenyl-Sepharose and interaction with a specific cellular target protein. The results suggest a novel application for GFP fusion proteins in the rapid, nonradioactive detection of interacting proteins on gel overlays.
维多利亚多管发光水母的绿色荧光蛋白（GFP）是一种用于原位和体内监测基因表达的新兴工具。由于其荧光特性，当GFP与特定的目标蛋白框内融合时，可以对该蛋白行为的各个方面进行非侵入性分析。在此，我们描述了GFP与人钙调蛋白样蛋白（CLP）之间的融合，并表明该蛋白保留了荧光以及CLP的已知特性，包括与苯基琼脂糖的Ca（2 +）依赖性相互作用以及与特定细胞靶蛋白的相互作用。结果表明，GFP融合蛋白在凝胶覆盖物上相互作用蛋白的快速、非放射性检测中具有新的应用。
