Patrickios C S, Yamasaki E N
School of Chemistry and Molecular Sciences, University of Sussex, Falmer, Brighton, United Kingdom.
Anal Biochem. 1995 Oct 10;231(1):82-91. doi: 10.1006/abio.1995.1506.
Experimental isoelectric points and amino acid compositional data for 58 proteins were compiled and organized. The experimental isoelectric points correlated well with the acidic to basic amino acid molar ratio. This agreement proved the usefulness of a recently presented analytical expression correlating explicitly protein isoelectric point to acid-base composition. Regressed acidic and basic dissociation constants were determined to be pK(alpha) = 4.9 and pK(beta) = 10.0, in fair agreement with the expected values of pK(alpha) = 4.2 and pK(beta) = 11.2. Theoretical isoelectric points determined by a more complete computational procedure were on the average in as good an agreement with the experimental values as those calculated via the theoretical approximation using the regressed dissociation constants. Thus, the analytical approximation is a powerful tool for the convenient and accurate calculation of protein isoelectric point from the amino acid composition.
整理并组织了58种蛋白质的实验等电点和氨基酸组成数据。实验等电点与酸性氨基酸和碱性氨基酸的摩尔比相关性良好。这一结果证明了最近提出的一个将蛋白质等电点与酸碱组成明确关联起来的分析表达式的实用性。回归得到的酸性和碱性解离常数分别为pK(α)=4.9和pK(β)=10.0,与预期值pK(α)=4.2和pK(β)=11.2相当吻合。通过更完整的计算程序确定的理论等电点与实验值的平均吻合程度,与使用回归解离常数通过理论近似计算得到的结果相当。因此,该分析近似法是一种从氨基酸组成方便且准确地计算蛋白质等电点的有力工具。