Donati R, Sabolovic N, Wellman M, Artur Y, Siest G
Centre du Médicament, UA CNRS No. 597, Nancy, France.
Clin Chim Acta. 1988 May 31;174(2):149-61. doi: 10.1016/0009-8981(88)90382-8.
Eight hybridoma clones secreting large amounts of monoclonal antibodies against purified human kidney gamma-glutamyltransferase (GGT) were isolated and produced in ascites. None of them inhibits the catalytic activity of GGT. They all bind to the heavy subunit of this dimeric enzyme. Immunoblot analysis showed that these antibodies react with the catalytically active GGT. The monoclonal antibodies also recognize the heavy subunit of the human liver enzyme. This is of interest, as serum GGT is known to originate from the liver. None of the monoclonals reacts with GGTs from rat or pig kidney. After identification of epitopes specificities, the antibodies will be used for the development of immunoassays of GGT especially in human serum.
分离出八个分泌大量抗纯化人肾γ-谷氨酰转移酶（GGT）单克隆抗体的杂交瘤克隆，并在腹水中产生。它们均不抑制GGT的催化活性。它们都与这种二聚体酶的重亚基结合。免疫印迹分析表明，这些抗体与具有催化活性的GGT发生反应。这些单克隆抗体还识别人类肝脏酶的重亚基。这很有意思，因为已知血清GGT源自肝脏。没有一种单克隆抗体与大鼠或猪肾的GGT发生反应。在确定表位特异性后，这些抗体将用于开发GGT免疫测定法，尤其是用于人血清中的GGT免疫测定。
