Fiebig H, Behn I, Hommel U
Bereich Immunbiologie, Karl-Marx-Universität Leipzig.
Allerg Immunol (Leipz). 1989;35(3):203-12.
The binding properties of a monoclonal antibody to an early activation marker of human lymphocytes are described. The monoclonal antibody BL-Ac/p26 binds to an antigen which is expressed on activated lymphocytes. This antigen is not detectable on resting lymphocytes or other blood cells. The surface radioiodinated antigen of activated T cells isolated by the monoclonal antibody BL-Ac/p26 is separated by SDS-PAGE in a major 26k Da component and a minor band (32 kDa) under reducing conditions. These polypeptide chains form disulphide linked dimers on the cell surface (Mr 55-77 kDa). This 26 kDa antigen is a very early activation marker of T lymphocytes. Human T lymphocytes stimulated by mitogens (PHA, ConA or PWM), anti-TCR/CD3 monoclonal antibodies or allogeneic leucocytes express this 26 kDa antigen after 2-4 hours.
本文描述了一种单克隆抗体与人淋巴细胞早期激活标志物的结合特性。单克隆抗体BL-Ac/p26与活化淋巴细胞上表达的一种抗原结合。在静息淋巴细胞或其他血细胞上无法检测到这种抗原。在还原条件下,通过单克隆抗体BL-Ac/p26分离的活化T细胞表面放射性碘化抗原经SDS-PAGE分离,主要为26 kDa成分,还有一条次要条带(32 kDa)。这些多肽链在细胞表面形成二硫键连接的二聚体(Mr 55 - 77 kDa)。这种26 kDa抗原是T淋巴细胞非常早期的激活标志物。经丝裂原(PHA、ConA或PWM)、抗TCR/CD3单克隆抗体或同种异体白细胞刺激的人T淋巴细胞在2 - 4小时后表达这种26 kDa抗原。