链激酶完整N端结构域的表达与特性分析
Expression and characterization of the intact N-terminal domain of streptokinase.
作者信息
Azuaga A I, Woodruff N D, Conejero-Lara F, Cox V F, Smith R A, Dobson C M
机构信息
Oxford Centre for Molecular Sciences and New Chemistry Laboratory, University of Oxford, United Kingdom.
出版信息
Protein Sci. 1999 Feb;8(2):443-6. doi: 10.1110/ps.8.2.443.
Proteolytic studies have enabled two of the three putative domains of the fibrinolytic protein streptokinase to be isolated and characterized (Conejero-Lara F et al., 1996, Protein Sci 5:2583-2591). The N-terminal domain, however, could not be isolated in these experiments because of its susceptibility to proteolytic cleavage. To complete the biophysical characterization of the domain structure of streptokinase we have overexpressed, purified, and characterized the N-terminal region of the protein, residues 1-146. The results show this is cooperatively folded with secondary structure content and overall stability closely similar to those of the equivalent region in the intact protein.
蛋白水解研究已使纤溶蛋白链激酶三个推定结构域中的两个得以分离和表征（科内耶罗 - 拉拉F等人，1996年，《蛋白质科学》5：2583 - 2591）。然而，在这些实验中未能分离出N端结构域，因为它易受蛋白水解切割。为了完成链激酶结构域结构的生物物理表征，我们对该蛋白的N端区域（第1至146位残基）进行了过表达、纯化和表征。结果表明，该区域协同折叠，其二级结构含量和整体稳定性与完整蛋白中相应区域的二级结构含量和整体稳定性非常相似。
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