ausblenden:
Schlagwörter:
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Zusammenfassung:
1. The effect of different ATP concentrations on the inhibition of purified membrane-bound Na+-K+-ATPase by different inhibitors was investigated.
2. Trypsin, the SH-group reagent 5,5'dithiobis(2-nitrobenzoic acid) and the covalently binding ATP analogue 6-((3-carboxy-4-nitrophenyl)thiol)-9-β-d-ribofuranosyl-purine 5'triphosphate were employed as inhibitors.
3. The effects of ATP on enzyme inhibition were observed in three concentration ranges different from those previously employed to determine the high affinity ATP binding.
4. The data suggest that four types of nucleotide binding sites are present on the Na+-K+-ATPase molecule.
