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The calmodulin-stimulated ATPase of maize coleoptiles is a 140000-Mrpolypeptide

✍ Scribed by Sally A. Briars; Felix Kessler; David E. Evans

Book ID
104753063
Publisher
Springer-Verlag
Year
1988
Tongue
English
Weight
406 KB
Volume
176
Category
Article
ISSN
0032-0935

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✦ Synopsis

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 (Β±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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## Summary Maize actin‐depolymerizing factor, ZmADF, binds both G‐ and F‐actin and enhances __in vitro__ actin dynamics. Evidence from studies on vertebrate ADF/cofilin supports the view that this class of protein responds to intracellular and extracellular signals and causes actin reorganization.