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首页> 外文期刊>The protein journal >Enzymatic properties of newly found green turtle egg white ribonuclease.
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Enzymatic properties of newly found green turtle egg white ribonuclease.

机译：新发现的绿turtle卵蛋白核糖核酸酶的酶学性质。

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摘要

Egg white ribonuclease was first found in green turtle eggs. The general properties were studied on substrate specificity, the optimum pH and temperature, and the effect of pH and temperature on the RNase activity. The enzyme studied was specific for poly (C) and degraded poly (U) at the lower rate and had the pH optimum at 7.0 and the optimum temperature at 40 degrees C. It was stable at alkaline range (pH 8.0-10.0) and up to 60 degrees C in pH 9.0 for 1 h, and unstable at acidic side for all temperatures. All of the properties studied showed similarity to RNase A. However, the optimum pH, broad range of optimum temperature and pH stability were different from RNase A. To evaluate the relationship of the structure and enzymatic properties, the 3D-structure of this enzyme was engineered by program MODELLER using two RNases (2BWL and 2BLZ) as starting models. The differences found in activity might be affected from the structure of micro environmental changing caused by amino acids deletion and substitution on the molecule.
机译：蛋清核糖核酸酶首先在绿龟蛋中发现。研究了底物特异性，最适pH和温度以及pH和温度对RNase活性的影响的一般特性。所研究的酶在较低的速率下对聚（C）和降解的聚（U）具有特异性，并且具有7.0的最佳pH和40摄氏度的最佳温度。在碱性范围（pH 8.0-10.0）和更高的温度下稳定到60摄氏度，pH 9.0保持1小时，并且在酸性条件下在所有温度下均不稳定。所研究的所有特性均与RNase A相似。但是，最佳pH，最适温度范围和pH稳定性与RNase A不同。为评估结构与酶学性质的关系，该酶的3D结构为由程序MODELLER使用两个RNase（2BWL和2BLZ）作为起始模型进行设计。在活性上发现的差异可能受分子上氨基酸缺失和取代引起的微环境变化结构的影响。

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