Huang L W, Liu H W, Chang K L
School of Technology for Medical Sciences, Kaohsiung Medical University, Taiwan.
Hybridoma. 2001 Feb;20(1):53-7. doi: 10.1089/027245701300060463.
Human arginase was purified from liver and two monoclonal antibodies (MAbs), HA1 and HA2, were produced by fusion of spleen cells from an arginase-immunized BALB/c mouse and the NS-1 myeloma cell line. Both MAbs were of the IgG3 subclass and contained the kappa light chain. HA1 inhibited arginase activity, suggesting that it binds to the arginase catalytic site. HA1 and a horseradish peroxidase-conjugated polyclonal rabbit anti-human arginase antibody were used to develop a sandwich enzyme-linked immunoadsorbent assay (ELISA) for the quantification of human arginase, which can be used in the 1 to 300 ng/mL range. Because of its sensitivity and specificity, this MAb can be successfully applied to the ELISA quantification of arginase in serum and culture supernatants.
从肝脏中纯化出人类精氨酸酶，并通过将来自精氨酸酶免疫的BALB/c小鼠的脾细胞与NS-1骨髓瘤细胞系融合，制备了两种单克隆抗体（MAb），即HA1和HA2。两种单克隆抗体均属于IgG3亚类，含有κ轻链。HA1抑制精氨酸酶活性，表明它与精氨酸酶催化位点结合。HA1和辣根过氧化物酶偶联的多克隆兔抗人精氨酸酶抗体用于开发一种夹心酶联免疫吸附测定（ELISA），用于定量人精氨酸酶，其可在1至300 ng/mL范围内使用。由于其敏感性和特异性，这种单克隆抗体可成功应用于血清和培养上清液中精氨酸酶的ELISA定量。
