Plant and Cell Physiology, 1982, Vol. 23, No. 3 385-395
© 1982
Article |
Specific Increase in Phosphatase Isozymes in Cucumber Roots Caused by Calcium Deficiency
Institute for Agricultural and Biological Sciences, Okayama University Chuo 2-20-1, Kurashiki, Okayama 710, Japan
Phosphatases in cucumber roots, whose production was induced by Ca2$ deficiency, were characterized chromatographically using ATP, 2'(3')-AMP and p-nitrophenyl-phosphate (PNPP) as substrates. Ca2$ deficiency stimulated greater than 10-fold increases in the activities with these substrates of the non-adsorbed fraction from a DEAE-cellulose column. Several fractions associated with these phosphatase activities were eluted from the column with NaCl solution; their levels increased less with Ca2$ starvation. When the non-adsorbed fraction from Ca2$-straved roots was applied to a Sephadex G-200 column, fractions associated with 2'(3')-AMPase (phosphatase I) and with both ATPase and PNPPase (phosphatase II) were separated. In the control roots, very weak activities of phosphatases I and II were observed at the same position on the gel filtration. The phosphatase I isolated from both the control and Ca2$-starved roots was extremely specific to nucleoside 2'(3')-monophosphates, whereas phosphatase II from both types of roots had a relatively broad substrate specificity. When phosphatase I from Ca2$-starved roots was stained with 2'(3')-AMP in CaCl2 after polyacrylamide gel electrophoresis, a single band was obtained. Phosphatase I from control roots also showed a single band, with the same Rf value. Phosphatase II from both types of roots contained two isozyme bands when the activities were stained with either ATP or PNPP. These results indicate that Ca2$ starvation causes specific increases in the level of phosphatases I and II in cucumber roots.
(Received October 28, 1981; Accepted January 19, 1982)
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