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Inhibition of mitochondrial ATPase by dicarbopolyborate, a new enzyme inhibitor
Polyborate anions were found to inhibit mitochondrial ATPase. Mercapto and chloro derivatives of dicarbononaborates showed full inhibition of the enzyme activity at 0.5-0.8 mM. The inhibitory effect of dodecaborates was lower. The inhibition was of competitive type with respect to ATP. The inhibitio...
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Published in: | Journal of bioenergetics and biomembranes 1994-10, Vol.26 (5), p.583-586 |
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container_end_page | 586 |
container_issue | 5 |
container_start_page | 583 |
container_title | Journal of bioenergetics and biomembranes |
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creator | Drahota, Z Mares, V Rauchová, H Saf, P Kalous, M |
description | Polyborate anions were found to inhibit mitochondrial ATPase. Mercapto and chloro derivatives of dicarbononaborates showed full inhibition of the enzyme activity at 0.5-0.8 mM. The inhibitory effect of dodecaborates was lower. The inhibition was of competitive type with respect to ATP. The inhibition of soluble F1-ATPase indicates a direct interaction of the polyborate anion with the catalytic part of the enzyme molecule. |
doi_str_mv | 10.1007/BF00762743 |
format | article |
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Mercapto and chloro derivatives of dicarbononaborates showed full inhibition of the enzyme activity at 0.5-0.8 mM. The inhibitory effect of dodecaborates was lower. The inhibition was of competitive type with respect to ATP. 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language | eng |
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subjects | Animals Boron Compounds - chemistry Boron Compounds - pharmacology Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology Kinetics Mitochondria, Liver - enzymology Models, Molecular Proton-Translocating ATPases - antagonists & inhibitors Rats Structure-Activity Relationship |
title | Inhibition of mitochondrial ATPase by dicarbopolyborate, a new enzyme inhibitor |
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