Jensen L E, Petersen T E, Thiel S, Jensenius J C
Department of Medical Microbiology and Immunology, University of Aarhus, Denmark.
Dev Comp Immunol. 1995 Jul-Aug;19(4):305-14. doi: 10.1016/0145-305x(95)00010-q.
Serum amyloid P-component (SAP) is a glycoprotein consisting of five or ten noncovalently associated identical subunits of molecular weight 19,000-30,000. Herein we report the isolation and partial characterization of a SAP-like protein from rainbow trout serum. The protein was isolated by calcium-dependent binding to Sepharose followed by ion-exchange and size-exclusion chromatography. Rabbit antibody against human SAP reacted with the trout protein and the NH2-terminal sequence of 16 amino acids showed 60% identity with the first 15 residues of human SAP. SDS-PAGE and endoglycosidase treatment indicated that the trout protein is a glycoprotein in which five or six subunits are linked by disulphide bonds. The subunits have a molecular weight of 37,000 of which approximately 13% is due to carbohydrate. We propose to name the trout protein sulphide linked SAP (SL-SAP).
血清淀粉样蛋白P成分(SAP)是一种糖蛋白,由五个或十个分子量为19,000 - 30,000的非共价结合的相同亚基组成。在此我们报告从虹鳟鱼血清中分离出一种类似SAP的蛋白及其部分特性。该蛋白通过与琼脂糖凝胶的钙依赖性结合进行分离,随后进行离子交换和尺寸排阻色谱法。抗人SAP的兔抗体与鳟鱼蛋白发生反应,其16个氨基酸的NH2末端序列与人类SAP的前15个残基具有60%的同一性。SDS - PAGE和内切糖苷酶处理表明,鳟鱼蛋白是一种糖蛋白,其中五个或六个亚基通过二硫键相连。这些亚基的分子量为37,000,其中约13%归因于碳水化合物。我们建议将鳟鱼蛋白命名为硫化连接的SAP(SL - SAP)。