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Plant Physiology 71:594-597 (1983)
© 1983 American Society of Plant Biologists

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Articles

Membrane-Associated ATPases in Isolated Secretory Vesicles 1

Lynne L. W. Binari and Richard H. Racusen

Department of Botany, University of Maryland, College Park, Maryland 20742

Polysaccharide-containing vesicles were collected from secretory cells maintained in liquid culture. Characterization of membrane-associated nucleosidephosphatases revealed that the vesicles specifically hydrolyze ATP, have a pH optimum between 6.0 and 6.5, and are stimulated by inorganic cations, especially K+. The ATPase activity in these vesicles was inhibited by orthovanadate and N,N'-dicyclohexylcarbodiimide; other inhibitors, such as oligomycin, sodium azide, and diethylstilbestrol were generally ineffective. Results from these studies are consistent with the notion that vesicles derived from the Golgi apparatus have partially differentiated into plasmalemma before they fuse with the plasma membrane.

1 Scientific Article No. A-3307, Contribution No. 6379 of the Maryland Agricultural Experiment Station, College Park, MD.






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ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1983 by the American Society of Plant Biologists