Plant Physiol.
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Plant Physiology 77:124-128 (1985)
© 1985 American Society of Plant Biologists

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Articles

Spinach Nitrate Reductase

Purification, Molecular Weight, and Subunit Composition

Hiroki Nakagawa, Yasuhiro Yonemura, Hiroyasu Yamamoto, Takahide Sato, Nagao Ogura and Ryo Sato

Department of Agricultural Chemistry, Faculty of Horticulture, Chiba University, Matsudo, Chiba 271, Japan, Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan

Nitrate reductase was purified about 3,000-fold from spinach leaves by chromatography on butyl Toyopearl 650-M, hydroxyapatite-brushite, and blue Sepharose CL-6B columns. The purified enzyme yielded a single protein band upon polyacrylamide gel electrophoresis under nondenaturing conditions. This band also gave a positive stain for reduced methylviologen-nitrate reductase activity. The specific NADH-nitrate reductase activities of the purified preparations varied from 80 to 130 units per milligram protein. Sucrose density gradient centrifugation and gel filtration experiments gave a sedimentation coefficient of 10.5 S and a Stokes radius of 6.3 nanometers, respectively. From these values, a molecular weight of 270,000 ± 40,000 was estimated for the native reductase. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the denatured enzyme yielded a subunit band having a molecular weight of 114,000 together with a very faint band possessing a somewhat smaller molecular weight. It is concluded that spinach nitrate reductase is composed of two identical subunits possessing a molecular weight of 110,000 to 120,000.






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Copyright © 1985 by the American Society of Plant Biologists