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Updated: May 6, 2026

Discrimintion and Mapping of the Primary and Processed Transcripts in Maize Mitochondrion Using a Circular RT-PCR-based Strategy
Published on: July 29, 2019
The calmodulin-stimulated ATPase of maize coleoptiles is a 140000-Mr polypeptide
S A Briars1, F Kessler, D E Evans
1Department of Plant Sciences, University of Oxford, South Parks Road, OX1 3RA, Oxford, UK.
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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