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Plant and Cell Physiology, 1985, Vol. 26, No. 1 35-46
© 1985

Article

Comparisons of Plasma Membranes from Shoots and Roots of Winter Rye (Secale cereale L. cv. Puma): Polypeptide Composition, ATPase Activity and Specific Naphthylphthalamic Acid Binding Capacity1

Matsuo Uemura and Shizuo Yoshida

The Institute of Low Temperature Science, Hokkaido University Sapporo 060, Japan

Polypeptide compositions, ATPase characteristics, and the N-1-naphthylphthalamic acid binding capacity of plasma membranes prepared from winter rye (Secale cereale L. cv. Puma) shoots and roots were examined and compared.

Some unique polypeptides were revealed in each plasma membrane by one- and two-dimensional slab gel electrophoresis. A difference was also detected in glycopeptide compositions. The plasma membranes from both organs contained Mg2+-stimulated ATPase exhibiting slightly different properties in the divalent cation specificity and the kinetic constants. The ATPase activities from both organs showed a similar optimum pH around 6.5, simple Michaelis-Menten saturation with increasing ATP-Mg concentrations, and little K+-stimulation at the optimum pH. Both ATPases were inhibited by orthovanadate, however, the degree of inhibition was a little different in each membrane sample. The specific N-1-naphthylphthalamic acid binding capacity in the shoot plasma membrane was 2.6-fold higher than that in the root plasma membrane.

These results suggest that polypeptide compositions of plasma membranes vary corresponding with a difference in the physiological functions of plasma membranes between shoots and roots of winter rye.

1 Contribution No. 2670 from the Institute of Low Temperature Science.

(Received May 17, 1984; Accepted October 9, 1984)
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