人血小板和内皮血小板反应蛋白之间的结构与免疫学差异。

Structural and immunological differences between human platelet and endothelial thrombospondins.

作者信息

Clezardin P, Hunter N R, McGregor J L, Pepper D S, Dawes J

出版信息

FEBS Lett. 1986 Feb 3;196(1):49-53. doi: 10.1016/0014-5793(86)80212-5.

Abstract

The structural and immunological properties of human thrombospondins isolated from platelets and from endothelial cells were compared. Both thrombospondins were digested with either trypsin or thermolysin, in the presence or absence of calcium, then injected onto a Superose 12 gel filtration column. The isolated thermolysin-generated fragments of thrombospondins were identified by radioimmunoassays using either different monoclonal antibodies or a polyclonal antibody directed against platelet thrombospondin. The results show that platelet and endothelial thrombospondins are both partially protected from trypsin digestion in the presence of calcium but have different trypsin and thermolysin fragmentation patterns. The thermolysin-generated fragments from platelet and endothelial thrombospondins are recognized differently by a monoclonal antibody whereas all of them are identified by a polyclonal antibody.

摘要

对从血小板和内皮细胞中分离出的人血小板反应蛋白的结构和免疫特性进行了比较。两种血小板反应蛋白在有或没有钙存在的情况下，用胰蛋白酶或嗜热菌蛋白酶进行消化，然后注入Superose 12凝胶过滤柱。使用不同的单克隆抗体或针对血小板血小板反应蛋白的多克隆抗体，通过放射免疫测定法鉴定分离出的嗜热菌蛋白酶产生的血小板反应蛋白片段。结果表明，在有钙存在的情况下，血小板和内皮细胞血小板反应蛋白都能部分免受胰蛋白酶消化，但具有不同的胰蛋白酶和嗜热菌蛋白酶裂解模式。血小板和内皮细胞血小板反应蛋白的嗜热菌蛋白酶产生的片段被一种单克隆抗体以不同方式识别，而所有这些片段都能被一种多克隆抗体识别。