Quantitative Elisa for Human Lactate Dehydrogenase Isoenzyme 5
- 1 January 1988
- journal article
- research article
- Published by Taylor & Francis in Journal of Immunoassay
- Vol. 9 (1), 37-49
- https://doi.org/10.1080/01971528808053209
Abstract
Four monoclonal antibodies (Mab) derived from mice immunized with lactate dehydrogenase 5 (LDH5) react strongly with LDH5, but weakly with LDH2 which contains a single subunit of type M. Experimental evidence suggests that these antibodies are directed to an antigenic determinant in the interface between two subunits of type M. A sandwich ELISA procedure was devised, using these Mabs to identify and quantify LDH5. The procedure involves immobilization of one of these Mabs by its adsorption onto polyclonal anti-mouse IgG coated polystyrene plates, adsorption of LDH5, its identification by the same Mab as that used in the immobilization step, and finally color development by an enzyme labeled rabbit anti-mouse IgG antiserum. The method enables LDH5 to be assayed at a concentration range of 0–5 μg/ml.Keywords
This publication has 9 references indexed in Scilit:
- Direct measurement of creatine kinase-MB activity in serum after extraction with a monoclonal antibody specific to the MB isoenzyme.Clinical Chemistry, 1986
- Three-dimensional structure of an antigen–antibody complex at 6 Å resolutionNature, 1985
- Clinical biochemistry of lactate dehydrogenaseCell Biochemistry and Function, 1984
- Does lactate dehydrogenase isoenzyme-5 contribute to the predictive power of total lactate dehydrogenase in myocardial infarction?Clinical Chemistry, 1983
- Three-dimensional structure of d-glyceraldehyde-3-phosphate dehydrogenaseJournal of Molecular Biology, 1974
- Molecular symmetry axes and subunit interfaces in certain dehydrogenasesJournal of Molecular Biology, 1973