Kauffman D, Wong R, Bennick A, Keller P
Biochemistry. 1982 Dec 7;21(25):6558-62. doi: 10.1021/bi00268a036.
The complete amino acid sequence of a basic proline-rich protein, IB-9, from human parotid saliva was determined by automated Edman degradation of peptides obtained by enzymatic cleavage of the intact protein with clostripain. The protein was digested with papain and elastase to obtain overlapping peptides. Automated Edman degradation of the intact protein was also performed. The protein consists of 61 amino acids, of which 26 are proline residues. The partial sequence of another human parotid basic proline-rich protein, IB-6, was also obtained. With one exception the first 54 residues of the two proteins are identical. An exceptional degree of internal reiteration occurs in both molecules, including several repeated sequences of 12-14 amino acids. The proteins show a high degree of homology with the C-terminal portion of the salivary acidic proline-rich protein C.
通过用梭菌蛋白酶对完整蛋白质进行酶解获得肽段,并对这些肽段进行自动Edman降解,确定了来自人腮腺唾液的一种富含脯氨酸的碱性蛋白IB-9的完整氨基酸序列。用木瓜蛋白酶和弹性蛋白酶消化该蛋白质以获得重叠肽段。还对完整蛋白质进行了自动Edman降解。该蛋白质由61个氨基酸组成,其中26个是脯氨酸残基。还获得了另一种人腮腺富含脯氨酸的碱性蛋白IB-6的部分序列。除一个例外,这两种蛋白质的前54个残基是相同的。两种分子中都出现了异常程度的内部重复,包括几个12 - 14个氨基酸的重复序列。这些蛋白质与唾液酸性富含脯氨酸蛋白C的C末端部分具有高度同源性。