H-ATPase Activity from Storage Tissue of Beta vulgaris: IV. N,N'-Dicyclohexylcarbodiimide Binding and Inhibition of the Plasma Membrane H-ATPase.

Abstract:

:The molecular weight and isoelectric point of the plasma membrane H(+)-ATPase from red beet storage tissue were determined using N,N'-dicyclohexylcarbodiimide (DCCD) and a H(+)-ATPase antibody. When plasma membrane vesicles were incubated with 20 micromolar [(14)C]-DCCD at 0 degrees C, a single 97,000 dalton protein was visualized on a fluorograph of a sodium dodecyl sulfate polyacrylamide gel. A close correlation between [(14)C]DCCD labeling of the 97,000 dalton protein and the extent of ATPase inhibition over a range of DCCD concentration suggests that this 97,000 dalton protein is a component of the plasma membrane H(+)-ATPase. An antibody raised against the plasma membrane H(+)-ATPase of Neurospora crassa cross-reacted with the 97,000 dalton DCCD-binding protein, further supporting the identity of this protein. Immunoblots of two-dimensional gels of red beet plasma membrane vesicles indicated the isoelectric point of the H(+)-ATPase to be 6.5.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Oleski NA,Bennett AB

doi

10.1104/pp.83.3.569

subject

Has Abstract

pub_date

1987-03-01 00:00:00

pages

569-72

issue

3

eissn

0032-0889

issn

1532-2548

journal_volume

83

pub_type

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