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Production and characterization of separate monoclonal antibodies to human brain and erythrocyte acetylcholinesterases.

作者信息

Novales-Li P, Priddle J D

机构信息

Department of Pharmacology, University of Oxford, United Kingdom.

出版信息

Hybridoma. 1995 Feb;14(1):67-73. doi: 10.1089/hyb.1995.14.67.

DOI:10.1089/hyb.1995.14.67
PMID:7768534
Abstract

Four murine monoclonal antibodies (MAbs) of the IgM class were raised against human acetylcholinesterase (AChE; Ec 3.1.1.7). The MAbs BMS-3E4, BMS-7G10, and BMS-9F4 all recognized human erythrocyte AChE, while BMS-6D6 bound specifically to human soluble brain AChE, on the basis of immunobinding assays. Dose-response studies gave an ELISA ED50 titer of 4.5 x 10(-4) M for BMS-6D6, while BMS-3E4 gave the best titer at 8.8 x 10(-4) M. Sucrose density gradients demonstrated sedimentation of antigen-antibody complexes, consistent with earlier findings (i.e., BMS-6D6 bound with brain AChE while BMS-3E4 preferred erythrocyte (AChE). No cross-reactivity between the two MAbs against the two antigens was noted.

摘要

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