Plant and Cell Physiology Supplement
Supplement to Plant and Cell Physiology Vol. 47
Conference information

Purification and Characterization of SDS-dependent Protease from Barley Leaves
*Yasushi WatanabeToyoki AmanoYuzo Shioi
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Pages 679

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Abstract
The developmental transition in plant leaves, for example greening and senescence, is supported by precise regulation of protein synthesis and degradation. Therefore, investigation of proteases provides important information for plastid maturation. Previously we reported the protease activity in barley leaves. This activity was analyzed by Suc-Leu-Leu-Val-Tyr-MCA. These enzymes required sodium dodecyl sulfate (SDS) at concentrations of 0.1%. The activity with 0.1% SDS showed a good correlation with development and senescence of plastids. The enzyme was purified by the successive chromatography with DE52, Q Sepharose FF anion exchange, Hi Load Superdex 200, and Superdex 200 gel-filtration chromatography. Molecular weight of the enzyme was estimated to be approximately 35 k by SDS-PAGE. Additionally, this enzyme had maximum activity in neutral pH region. We are now under way on complete purification, amino acid sequence, inhibitor study, and substrate specificity to reveal enzymatic properties of this enzyme.
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© 2006 by The Japanese Society of Plant Physiologists
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