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Membrane-bound Adenosine Triphosphatase Activities of Oat Roots ¹

^a Department of Botany and Plant Pathology, Purdue University, Lafayette, Indiana 47907

Homogenates of oat (Avena sativa cv. Goodfield) roots contained at least five membrane-associated adenosine triphosphatase (ATPase) activities. The membrane-bound ATPases were separated on sucrose gradients and distinguished by membrane density, pH optima, sensitivity to monovalent salts, and substrate specificity.

A membrane fraction sedimenting at low centrifugal force (13,000g) contained two ATPase activities at pH 9.0. One membrane ATPase was coincident with cytochrome c oxidase activity and had a density of 1.18 grams per cubic centimeter. This membrane system was identified as mitochondria. The other pH 9.0 ATPase in this fraction occurred at a density of 1.16 grams per cubic centimeter. The identity of this membrane is unknown.

Three additional ATPases were in a membrane fraction sedimenting at high centrifugal forces (13,000-80,000g). One membrane ATPase coincided with NADH-cytochrome c reductase activity, had a density of about 1.09 grams per cubic centimeter, and was equally active at pH 6.0 and 9.0. A second membrane ATPase of the 13,000 to 80,000g fraction had a density of 1.13 grams per cubic centimeter and was more active at pH 9.0 than at pH 6.0. A third membrane ATPase had greater activity at pH 6.0 than at pH 9.0, and the membrane had an apparent density of 1.17 grams per cubic centimeter on the sucrose gradient. This ATPase was especially sensitive to KCI. The identity of the membranes which contain ATPases is discussed in relation to the distribution of other enzymes on the gradient.

³ Present address: Monsanto Chemical Company, 800 N. Lindbergh Boulevard, St. Louis, Mo. 63166.

¹ This research was supported by Grants GB-12674 and GB-31052X from the National Science Foundation. Journal Paper 4892 of the Purdue University Agricultural Experiment Station.

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