Open AccessDetection of enzyme polymorphism by using monoclonal antibodies.
Author(s) -
Clive A. Slaughter,
M. C. Coseo,
Michael P. Cancro,
Harry Harris
Publication year - 1981
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.78.2.1124
Subject(s) - monoclonal antibody , allele , microbiology and biotechnology , enzyme , antibody , polymorphism (computer science) , alkaline phosphatase , biology , monoclonal , chemistry , biochemistry , genetics , gene
Six monoclonal antibodies against human placental alkaline phosphate [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1], a highly polymorphic enzyme, were tested for reactivity against a panel of 295 placental extracts that had been typed electrophoretically. The products of the three common alleles as well as several rare alleles could be discriminated by the various antibodies. In some cases differences between allelic products were reflected by essentially "all-or-none" reactions, but in other cases the differences were smaller and demonstrable only by quantitative analysis of the binding. Evidence for allelic differences not detectable electrophoretically was also obtained.