Abstract
The calmodulin-stimulated ATPase of maize (Zea mays L.) coleoptiles has been purified by calcium-dependent binding to a calmodulin affinity column. In the presence of protease inhibitors (phenylmethylsulfonylfluoride and chymostatin) a polypeptide of relative molecular mass (Mr) 140000 (±10000) is obtained on sodium-dodecylsulphate polyacrylamide gels. This polypeptide is recognised specifically by an affinity-purified polyclonal antibody to mammalian calmodulin-stimulated calcium-pumping ATPases and is of similar Mr to the erythrocyte-membrane calcium pump (138000 Mr).
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Abbreviations
- EGTA:
-
ethylene glycol-bis(β-aminoethylether)-N,N,N′,N′-tetraacetic acid
- Mr :
-
apparent molecular mass
- SDS:
-
sodium dodecyl sulphate
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Briars, S.A., Kessler, F. & Evans, D.E. The calmodulin-stimulated ATPase of maize coleoptiles is a 140000-Mr polypeptide. Planta 176, 283–285 (1988). https://doi.org/10.1007/BF00392457
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DOI: https://doi.org/10.1007/BF00392457