The conformations of a functional spin-labeled derivative of gastric H/K-ATPase investigated by EPR spectroscopy.
A spin-labeled derivative of porcine gastric H/K-ATPase with high ATP hydrolyzing activity (77 mumol of Pi/(mg.h)) has been prepared. Over 65% of initial ATPase activity (115 mumol of Pi/(mg.h)) was preserved after complete reaction of the enzyme with the lysine reactive nitroxide spin-labeled TEMPO...
| Auteurs principaux: | , , |
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| Format: | Journal article |
| Langue: | English |
| Publié: |
1995
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