H/sup +/-ATPase activity from storage tissue of Beta vulgaris. IV. N,N'-dicyclohexylcarbodiimide binding and inhibition of the plasma membrane H/sup +/-ATPase

Journal Article · Sun Mar 01 04:00:00 EST 1987 · Plant Physiol.; (United States)

OSTI ID:6550876

Oleski, N A; Bennett, A B

The molecular weight and isoelectric point of the plasma membrane H/sup +/-ATPase from red beet storage tissue were determined using N,N'-dicyclohexylcarbodiimide (DCCD) and a H/sup +/-ATPase antibody. When plasma membrane vesicles were incubated with 20 micromolar (/sup 14/C)-DCCD at 0/sup 0/C, a single 97,000 dalton protein was visualized on a fluorography of a sodium dodecyl sulfate polyacrylamide gel. A close correlation between (/sup 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/sup +/-ATPase. An antibody raised against the plasma membrane H/sup +/-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/sup +/-ATPase to be 6.5.

• Research Organization: Univ. of California, Davis
• OSTI ID: 6550876
• Journal Information: Plant Physiol.; (United States), Journal Name: Plant Physiol.; (United States) Vol. 83:3; ISSN PLPHA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
BEETS
BIOCHEMICAL REACTION KINETICS
CARBON 14 COMPOUNDS
CELL CONSTITUENTS
CELL MEMBRANES
ELECTROPHORESIS
ENZYME ACTIVITY
FOOD
IMIDES
INHIBITION
ISOTOPE APPLICATIONS
KINETICS
LABELLED COMPOUNDS
LABELLING
MEMBRANES
MOLECULAR STRUCTURE
MOLECULAR WEIGHT
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PLANTS
PROTEINS
REACTION KINETICS
TRACER TECHNIQUES
VEGETABLES