The role of the plant plasma membrane H+-ATPase in K+ uptake was examined using red beet (Beta vulgaris L.) plasma membrane vesicles and a partially purified preparation of the red beet plasma membrane H+-ATPase reconstituted in proteoliposomes and planar bilayers. For plasma membrane vesicles, ATP-dependent K+ efflux was only partially inhibited by 100 [mu]M vanadate or 10 [mu]M carbonyl cyani...

Enzymatic heme oxygenase activity has been partially purified from extracts of the unicellular red alga Cyanidium caldarium, and the macromolecular components have been separated into three protein fractions, referred to as Fractions I, 11, and 111, by serial column chromatography through DEAE-cellulose and Reactive Blue 2-Sepharose. Fraction I is retained by DEAE-cellulose at low salt concentr...

A purified membrane fraction featuring ATPase activity was isolated from cotyledon tissue of Phaseolus vulgaris at different stages of germination. The fraction is enriched in both basal and Na(+)-K(+)-stimulated ATPase and is relatively free of contamination by fragments of mitochondrial membrane and microsomes. The isolated membranes have been tentatively identified as partially purified plas...

The subcellular distribution of Ca2+-activated, phospholipid-dependent protein kinase (Takai, Y., Kishimoto, A., Iwasa, Y., Kawahara, Y., Mori, T., and Nishia k a , Y. (1979) J. Biol. Chem 254, 3692-3695) in rat brain was investigated. Approximately one-third of the protein kinase was recovered in the soluble cytosol fraction, another one-third was in the crude mitochondrial fraction, and the r...