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富含脯氨酸蛋白(PRP)编码cDNA的分子克隆:PRP与C4b结合蛋白的一致性

Molecular cloning of the cDNA coding for proline-rich protein (PRP): identity of PRP as C4b-binding protein.

作者信息

Matsuguchi T, Okamura S, Aso T, Sata T, Niho Y

机构信息

First Department of Internal Medicine, Kyushu University, Fukuoka, Japan.

出版信息

Biochem Biophys Res Commun. 1989 Nov 30;165(1):138-44. doi: 10.1016/0006-291x(89)91045-0.

Abstract

Proline-rich protein (PRP) is a plasma protein with a high proportion of proline residues and possessing lipid-binding properties. In order to clarify its structure, a human liver cDNA library was screened using anti-PRP antiserum. Several overlapping phage cDNA clones were isolated and the total nucleotide sequence of the cDNA, 2178 bp in length, was analyzed. The amino acid composition of PRP deduced from the cDNA was essentially the same as that reported for PRP. In a homology search, the cDNA sequence was almost completely the same as the previously reported cDNA sequence of C4b-binding protein. Furthermore, the reported molecular weights of the two proteins under both reduced and unreduced conditions were quite alike. These findings indicate that PRP is identical with C4bp.

摘要

富含脯氨酸蛋白(PRP)是一种血浆蛋白,脯氨酸残基比例高且具有脂质结合特性。为了阐明其结构,使用抗PRP抗血清筛选人肝cDNA文库。分离出几个重叠的噬菌体cDNA克隆,并分析了长度为2178 bp的cDNA的总核苷酸序列。从cDNA推导的PRP氨基酸组成与报道的PRP基本相同。在同源性搜索中,cDNA序列与先前报道的C4b结合蛋白的cDNA序列几乎完全相同。此外,两种蛋白在还原和非还原条件下报道的分子量非常相似。这些发现表明PRP与C4bp相同。

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