Karn R C, Friedman R D, Merritt A D
Biochem Genet. 1979 Dec;17(11-12):1061-77. doi: 10.1007/BF00504345.
The acidic proline-rich proteins (Pr) showing genetic polymorphism were purified from human parotid salivas by gel filtration and ion exchange chromatography. Molecular weight determinations, amino acid composition analyses, and polypeptide mapping experiments indicate that the Pr 3 protein is a fragment of the Pr 1 protein. Studies of a parotid saliva factor capable of converting Pr 1 to Pr 3 and Pr 2 to Pr 4 indicate that Pr 3 and Pr 4 are generated from Pr 1 and Pr 2, respectively. Evidence suggests that the converting factor is a protease capable of posttranslationally cleaving Pr 1 and Pr 2, the primary or derived products of alleles Pr1 and Pr2.
通过凝胶过滤和离子交换色谱法从人腮腺唾液中纯化出显示遗传多态性的富含酸性脯氨酸的蛋白质(Pr)。分子量测定、氨基酸组成分析和多肽图谱实验表明,Pr 3蛋白是Pr 1蛋白的一个片段。对能够将Pr 1转化为Pr 3以及将Pr 2转化为Pr 4的腮腺唾液因子的研究表明,Pr 3和Pr 4分别由Pr 1和Pr 2产生。有证据表明,转化因子是一种蛋白酶,能够对Pr 1和Pr 2进行翻译后切割,Pr 1和Pr 2分别是等位基因Pr1和Pr2的主要产物或衍生产物。