Department of Biological Science and Technology, Institute of Technology and Science, The University of Tokushima Graduate School, Minami-Josanjima-cho, Tokushima 770-8506, Japan.
J Biosci Bioeng. 2013 Jan;115(1):15-9. doi: 10.1016/j.jbiosc.2012.08.001. Epub 2012 Aug 26.
A small heat shock protein, AgsA, possesses chaperone activity that can reduce the amount of heat-aggregated protein in vivo, and suppress the aggregation of chemical- and heat-denatured proteins in vitro. Therefore, we examined the ability of AgsA to stabilize the activity of several enzymes by using this chaperone activity. We observed that AgsA can stabilize the enzymatic activities of Renilla (Renilla reniformis) luciferase, firefly (Photinus pyralis) luciferase, and β-galactosidase, and showed comparable or greater stabilization of these enzymes than bovine serum albumin (BSA), a well-known stabilizer of enzyme activities. In particular, AgsA revealed better stabilization of Renilla luciferase and β-galactosidase than BSA under disulfide bond-reducing conditions with dithiothreitol. In addition, AgsA also increased the enzymatic performance of β-galactosidase and various restriction enzymes to a comparable or greater extent than BSA. These data indicate that AgsA may be useful as a general stabilizer of enzyme activities.
一种小的热休克蛋白 AgsA 具有伴侣活性，能够减少体内热聚集蛋白的量，并抑制体外化学和热变性蛋白的聚集。因此，我们利用这种伴侣活性来检查 AgsA 稳定几种酶活性的能力。我们观察到 AgsA 可以稳定海肾荧光素酶（Renilla reniformis）、萤火虫荧光素酶（Photinus pyralis）和β-半乳糖苷酶的酶活性，并且对这些酶的稳定作用与牛血清白蛋白（BSA）相当或更强，BSA 是一种众所周知的酶活性稳定剂。特别是，在含有二硫苏糖醇的还原条件下，AgsA 比 BSA 更能稳定海肾荧光素酶和β-半乳糖苷酶。此外，AgsA 还能提高β-半乳糖苷酶和各种限制酶的酶活性，其效果与 BSA 相当或更强。这些数据表明，AgsA 可能是一种有用的酶活性通用稳定剂。
