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Immunological Studies on ATPases in Mung Bean Hypocotyl Plasma Membrane: Proposal of the Presence of Two Molecular Species of ATPase

Immunological Studies on ATPases in Mung Bean Hypocotyl Plasma Membrane: Proposal of the Presence... Abstract ATPase in a highly purified plasma membrane fraction from mung bean hypocotyls was solubilized by lysolecithin and fractionated by glycerol density gradient centrifugation. Lysolecithin activated ATPase activity in the lower but not in the upper half of the activity peak after glycerol density gradient centrifugation. Antibody against maize root plasma membrane ATPase [Nagao et al. (1987) Plant Cell Physiol. 28: 1181] reacted to a 100-kDa polypeptide which was localized only at the lower half of the activity peak. Antibody against a 67-kDa polypeptide, which was proposed to be a subunit of a new type of ATPase in mung bean hypocotyl plasma membrane (Mito et al. the preceding paper), reacted only to its own antigen which was present mainly in the upper half of the activity peak. The activity peak fraction contained a low-molecular-mass polypeptide binding N.N′-dicyclohexylcarbodiimide. We propose the presence in mung bean hypocotyl plasma membrane of two distinct ATPases which differ from each other in polypeptide constitution and in their response to lysolecithin. This content is only available as a PDF. © 1988 The Japanese Society of Plant Physiologists (JSPP) http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant and Cell Physiology Oxford University Press

Immunological Studies on ATPases in Mung Bean Hypocotyl Plasma Membrane: Proposal of the Presence of Two Molecular Species of ATPase

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Publisher
Oxford University Press
Copyright
© 1988 The Japanese Society of Plant Physiologists (JSPP)
ISSN
0032-0781
eISSN
1471-9053
DOI
10.1093/oxfordjournals.pcp.a077576
Publisher site
See Article on Publisher Site

Abstract

Abstract ATPase in a highly purified plasma membrane fraction from mung bean hypocotyls was solubilized by lysolecithin and fractionated by glycerol density gradient centrifugation. Lysolecithin activated ATPase activity in the lower but not in the upper half of the activity peak after glycerol density gradient centrifugation. Antibody against maize root plasma membrane ATPase [Nagao et al. (1987) Plant Cell Physiol. 28: 1181] reacted to a 100-kDa polypeptide which was localized only at the lower half of the activity peak. Antibody against a 67-kDa polypeptide, which was proposed to be a subunit of a new type of ATPase in mung bean hypocotyl plasma membrane (Mito et al. the preceding paper), reacted only to its own antigen which was present mainly in the upper half of the activity peak. The activity peak fraction contained a low-molecular-mass polypeptide binding N.N′-dicyclohexylcarbodiimide. We propose the presence in mung bean hypocotyl plasma membrane of two distinct ATPases which differ from each other in polypeptide constitution and in their response to lysolecithin. This content is only available as a PDF. © 1988 The Japanese Society of Plant Physiologists (JSPP)

Journal

Plant and Cell Physiology – Oxford University Press

Published: Jul 1, 1988

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