H/sup +/-ATPase activity from storage tissue of Beta vulgaris. IV. N,N'-dicyclohexylcarbodiimide binding and inhibition of the plasma membrane H/sup +/-ATPase
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), Vol. 83:3
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
IMIDES
BIOCHEMICAL REACTION KINETICS
PROTEINS
LABELLING
MOLECULAR STRUCTURE
BEETS
CARBON 14 COMPOUNDS
CELL MEMBRANES
ELECTROPHORESIS
ENZYME ACTIVITY
INHIBITION
MOLECULAR WEIGHT
TRACER TECHNIQUES
CELL CONSTITUENTS
FOOD
ISOTOPE APPLICATIONS
KINETICS
LABELLED COMPOUNDS
MEMBRANES
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PLANTS
REACTION KINETICS
VEGETABLES
550201* - Biochemistry- Tracer Techniques