PURIFICATION OF PLACENTAL ALKALINE PHOSPHATASE AND ITS MONOCLONAL ANTIBODY

概要

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Synopsis Monoclonal antibodies (MAbs) to placental alkaline phosphatase (PA1P) were raised by using thehybridoma technique Spleen cells from immunized mice were fused with the mouse myeloma line NSI1using 50% polyethylene glycol and cultured in a selection medium Antibodies were screened by theenzyme immunoassay using immobilized solidlphase antigen and antilmouse immunogloblin Fab' (rabbit)!ylDIgalactosidase complex Four double,cloned hybridolnas were obtained The crosslreactivity withdifferent kinds of alkaline phosphatases of the raised MAbs was examined At nrst, MAb 11;DI10, withwhich placenta was stained but liver and small intestine were not stained in indirect immunonuorescence,was selected Then, the cross-reactivity of MAb 11-DI10 was further investigated by immunoblotting(Western blotting) MAb 1l4D410 reacted with PAlP but did not react with hepatic and intestinal alkalinephosphatase at all The binding activity of 125IIlabeled MAb 11.DI10 with different choriocarcinoma celllines (SCH, BeWo, NaUCCI1, NaUCC2, and NaUCCI3) was highest in SCH, then in the order of BeWo,NaUCCI3, NaUCCml and NaUCCI2, and correlated to the PA1P content of the cells (SCH > BeWo>NaUCCI3>NaUCCM1>NaUCC,2) Also the intensity of indirect immunonuorescence of the above cell lines withMAb 1llDI10 correlated with the PA1P content of each cell
社団法人日本産科婦人科学会の論文
1986-09-01