Kauffman D L, Bennick A, Blum M, Keller P J
Department of Oral Biology, University of Washington, Seattle 98195.
Biochemistry. 1991 Apr 9;30(14):3351-6. doi: 10.1021/bi00228a001.
Eleven basic proline-rich proteins were purified from the parotid saliva of a single individual. The complete amino acid sequences of six of these were determined by conventional protein sequence methodology, bringing to nine the number of known primary structures of nonglycosylated basic proline-rich proteins from the same individual. The partial sequence of one additional protein is also reported. All of the basic proline-rich proteins studied contain segments with identical or very similar sequences, but with two possible exceptions, none of the proteins is derived from another secreted proline-rich protein. The amino acid sequences of nine nonglycosylated basic proline-rich proteins were compared with primary structures deduced from published nucleotide sequences of DNA coding for human parotid proline-rich proteins. The sequences align well, in general, but differences also exist pointing to the complexity of the genetics of these proteins. Seven secretory basic proline-rich proteins appear to be formed from three larger precursors by selective posttranslational proteolyses of arginyl bonds. One of the basic proline-rich proteins appears to derive from human acidic proline-rich proteins. The remaining two proteins studied do not conform to any DNA structure as yet reported. Two of the basic proline-rich proteins studied are phosphoproteins and exhibit abilities to inhibit hydroxyapatite formation in vitro.
从一名个体的腮腺唾液中纯化出了11种富含脯氨酸的碱性蛋白。其中6种蛋白的完整氨基酸序列通过传统蛋白质测序方法得以确定，这使得来自该个体的非糖基化富含脯氨酸的碱性蛋白的已知一级结构数量达到了9种。还报道了另外一种蛋白的部分序列。所有研究的富含脯氨酸的碱性蛋白都含有相同或非常相似序列的片段，但可能有两个例外，没有一种蛋白是由另一种分泌的富含脯氨酸的蛋白衍生而来。将9种非糖基化富含脯氨酸的碱性蛋白的氨基酸序列与从已发表的编码人腮腺富含脯氨酸蛋白的DNA核苷酸序列推导的一级结构进行了比较。总体而言，序列匹配良好，但也存在差异，这表明这些蛋白的遗传复杂性。7种分泌性富含脯氨酸的碱性蛋白似乎是由三种较大的前体通过精氨酰键的选择性翻译后蛋白水解形成的。其中一种富含脯氨酸的碱性蛋白似乎源自人酸性富含脯氨酸蛋白。其余两种研究的蛋白不符合目前已报道的任何DNA结构。所研究的两种富含脯氨酸的碱性蛋白是磷蛋白，并在体外表现出抑制羟基磷灰石形成的能力。
