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Plant and Cell Physiology, 1992, Vol. 33, No. 4 363-369
© 1992

A Nitrate Reductase Inactivator Protein from Spinach. Purification, Molecular Weight and Subunit Composition

Tomoaki Yoshimura, Naoko Sekino, Katsuhiko Okuo, Takahide Sato, Nagao Ogura and Hiroki Nakagawa1

Department of Agricultural Chemistry, Faculty of Horticulture, Chiba University Matsudo, Chiba, 271 Japan

1 To whom correspond should be sent

A nitrate reductase-inactivator protein has been purified 16,000-fold from spinach leaves by pH 5 treatment, chromatography on SE53, Con A-Sepharose, and chromatofocusing. The yield was 12%, the specific activity was 115 units mg–1. Polyacrylamide gel electrophoresis of the final purified inactivator fraction yielded 2 major protein bands and both bands exhibited nitrate reductase-inactivator activity. Analysis of this inactivator protein by gel filtration and SDS-gel electrophoresis revealed protein stainable material only in a molecular weight range of 110,000–115,000. SDS gel electrophoresis under reducing conditions yielded 2 protein bands corresponding to molecular weights of 51,000 and 53,000. The proteolytic mapping for the two separated subunits appeared similar and possibly identical.

(Received October 28, 1991; Accepted February 24, 1992)
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