Inactivation of human lactate dehydrogenase isozymes by sulfhydryl reagents
| Autor: | Constance D. Anderson, Bruce M. Anderson |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
chemistry.chemical_classification
L-Lactate Dehydrogenase Organomercury Compounds Sulfhydryl Reagents Biophysics Cell Biology Fluoresceins Biochemistry Isozyme Isoenzymes Dissociation constant Kinetics Structure-Activity Relationship chemistry.chemical_compound Enzyme chemistry Lactate dehydrogenase Humans Enzyme kinetics NAD+ kinase Fluorescein Molecular Biology Maleimide |
| Zdroj: | Analytical Biochemistry. 161:258-261 |
| ISSN: | 0003-2697 |
| DOI: | 10.1016/0003-2697(87)90449-0 |
| Popis: | Human lactate dehydrogenase isozymes, LDH-1 and LDH-5, were inactivated at 25 degrees C and pH 7.5 by N-alkylmaleimides of varying chain length, and by fluorescein mercuric acetate. Second-order rate constants for the inactivation of LDH-5 by N-alkylmaleimides increased with increasing chain length of the maleimide derivative while essentially no chain-length effect was observed in the inactivation of LDH-1. Both isozymes were effectively inactivated by low concentrations of fluorescein mercuric acetate, and in both cases saturation kinetics were observed. Dissociation constants obtained from double-reciprocal plotting methods indicated a twofold better binding of fluorescein mercuric acetate to LDH-1. Protection from fluorescein mercuric acetate by NAD was observed with both enzymes. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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