The calmodulin-stimulated ATPase of maize coleoptiles is a 140000-Mr polypeptide期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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The calmodulin-stimulated ATPase of maize coleoptiles is a 140000-Mr polypeptide

Authors:	Sally A Briars Felix Kessler David E Evans

Institution:	(1) Department of Plant Sciences, University of Oxford, South Parks Road, OX1 3RA Oxford, UK;(2) Laboratorium für Organische Chemie, Eidgenössiche Technische Hochschule, Universitätsstrasse 16, CH-8092 Zürich, Switzerland

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 (M_r) 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 M_r to the erythrocyte-membrane calcium pump (138000 M_r).Abbreviations EGTA ethylene glycol-bis(-aminoethylether)-N,N,N,N-tetraacetic acid - M_r apparent molecular mass - SDS sodium dodecyl sulphate

Keywords:	Calmodulin-stimulated ATPase Plasma membrane (Ca²⁺ transport) Zea (Ca²⁺ transport)
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