Quantitative aspects of the interaction between ouabain and (Na + K)-activated ATPase in vitro |
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| Authors: | Tai Akera |
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| Affiliation: | 1. Department of Pharmacology, School of Medicine, Keio University, Tokyo, Japan;2. Department of Pharmacology, Michigan State University, East Lansing, Mich. U.S.A. |
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| Abstract: | The inhibitory effect of ouabain on (Na+ + K+)-activated ATPase (Mg2+-dependent, (Na+ + K+)-activated ATP phosphohydrolase, EC 3.6.1.3) obtained from rat brain microsomal fraction was re-examined using a modified method to estimate the inhibited reaction velocity. This method involves a preincubation of a ouabain-enzyme mixture in the presence of Na+, Mg2+ and ATP to bring the ouabain-enzyme reaction to near equilibrium. The (Na+ + K+)-activated ATPase reaction was subsequently started by the addition of a KCl solution. |
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| Keywords: | PCMB, p-chloromercuribenzoate S/M ratio, the ratio between the concentration of ouabain in the 100 000 × g sediment and that in the medium |
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