Immunological crossreactivity between the retinal Na(+)-Ca2+,K+ and the cardiac Na(+)-Ca2+ exchanger proteins
| Autor: | Hartmut Porzig, Regula Gutknecht |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Physiology
medicine.drug_class Immunoblotting Biophysics Heterologous Enzyme-Linked Immunosorbent Assay Nerve Tissue Proteins Cross Reactions Monoclonal antibody Homology (biology) Epitope Sodium-Calcium Exchanger law.invention chemistry.chemical_compound Epitopes law Retinal Rod Photoreceptor Cells medicine Animals Brain Chemistry medicine.diagnostic_test Myocardium Sodium Antibodies Monoclonal Retinal Cell Biology Intracellular Membranes Molecular biology Structural homology Biochemistry chemistry Immunoassay Recombinant DNA Calcium Cattle Carrier Proteins |
| Zdroj: | The Journal of membrane biology. 135(1) |
| ISSN: | 0022-2631 |
| Popis: | We have used a series of monoclonal antibodies (mAbs) to determine the degree of microscopic structural homology between the retinal Na(+)-Ca2+,K+ and the cardiac Na(+)-Ca2+ exchange proteins. Sets of mAbs were raised separately to partially purified preparations of either the retinal or the recombinant myocardial exchanger. Each panel of mAbs was then screened for crossreactivity with the respective heterologous exchanger using enzyme-linked immunoassay and immunoblotting techniques. Out of 43 anti-retinal exchanger mAbs, we found 3 detecting the cardiac exchanger on immunoblots, while 4 out of 36 anti-cardiac exchanger mAbs reacted with the retinal exchanger. The strength of the crossreactions was generally weak and suggested that only low affinity epitopes were available on the heterologous proteins. For two crossreacting anti-retinal mAbs the apparent binding affinities to the cardiac exchanger were lower by more than two orders of magnitude. The overall low degree of epitope sharing among the two sets of mAbs confirms that in spite of their obvious functional and topological similarities, microscopic structural homologies between the two proteins are scarce. |
| Databáze: | OpenAIRE |
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