Plant Physiol. Illumina
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Plant Physiology 59:1059-1063 (1977)
© 1977 American Society of Plant Biologists

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Articles

Proteases of Senescing Oat Leaves

I. Purification and General Properties

Rolf H. Drivdahl1 and Kenneth V. Thimann

a Thimann Laboratories, University of California, Santa Cruz, California 95064

Two proteases active in the senescing first leaves of oat seedlings (Avena sativa cv. Victory) have been purified approximately 500-fold by a combination of ammonium sulfate precipitation, affinity chromatography on hemoglobin-Sepharose, and ion exchange chromatography on DEAE-Sephadex. The enzymes show pH optima of 4.2 and 6.6 with denatured hemoglobin as substrate, and the molecular weights of both are about 76,000. Their optimum temperatures are close to 50 C. Small amounts of a third enzyme, active at pH 3.5, may also be present. The enzyme active at pH 6.6 shows evidence of a sulfhydryl residue in the active site.

1 Present address: Dept. of Agricultural Biochemistry, Washington State University, Pullman, Wash.






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ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1977 by the American Society of Plant Biologists