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Plant Physiology 58:447-452 (1976)
© 1976 American Society of Plant Biologists

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Articles

Microbody Malate Dehydrogenase Isozyme in Cotyledons of Cucumis sativus L. during Development 1

Irene M. Wainwright2 and Irwin P. Ting

a Department of Biology, University of California, Riverside, California 92502

The properties of the microbody malate dehydrogenase (EC 1.1.1.37) (MDH) isozyme from cotyledons of Cucumus sativus L. were compared during development. It is concluded that the isozyme remains unaltered, despite the transition from glyoxysomal to peroxisomal function that occurs during greening of the cotyledons. This conclusion is based on electrophoretic behavior, chromatographic elution from DEAE-cellulose, molecular weight, kinetic behavior, and immunological identity. In most cases, the distinct properties of the other MDH isozymes in the tissue during development provide additional support for an unchanging microbody isozyme. A method for assaying specifically the microbody isozyme was developed; a diluted preparation was assayed spectrophotometrically before and after complete immunological precipitation. The turnover of the microbody MDH isozyme was investigated by a radioactive labeling study. There is incorporation into both glyoxysomal and peroxisomal MDH. Degradation rates do not correspond with either decline of glyoxysomal activity or the continuation of peroxisomal activity. Apparently, the microbody MDH isozyme is continually turned over throughout cotyledon development.

2 Recipient of Phi Beta Kappa grant.

1 This work was supported in part by National Science Foundation Grant BMS74-11842.






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Copyright © 1976 by the American Society of Plant Biologists