Plant Physiol. Drug Metab Dispos
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PLANT PHYSIOLOGY , Vol 107, Issue 2 401-405, Copyright © 1995 by American Society of Plant Biologists

BIOCHEMISTRY AND ENZYMOLOGY

Light-Induced Chloroplast [alpha]-Amylase in Pearl Millet (Pennisetum americanum)

KJM. Vally and R. Sharma
School of Life Sciences, University of Hyderabad, Hyderabad-500134, India

In pearl millet (Pennisetum americanum) seedlings light induces the appearance of a leaf [alpha]-amylase isozyme. The leaf [alpha]-amylase isozyme was present in enriched amounts in isolated chloroplast but it could not be detected in isolated etioplasts. The chloroplast [alpha]-amylase was present in both mesophyll and bundle-sheath chloroplasts. Preliminary characterization indicated that molecular properties of chloroplast [alpha]-amylase were like those of a typical [alpha]-amylase. The plastidic [alpha]-amylase had a molecular mass of 46 kD, pH optimum of 6.2, required Ca2+ for activity and thermostability, but lost activity in the presence of ethylenediaminetetracetate. Plastidic [alpha]-amylase activity after sodium dodecyl sulfate-polyacrylamide gel electrophoresis could be renatured in situ by Triton X-100. Western blot analysis demonstrated that this protein was antigenically similar to a maize seed [alpha]-amylase. In vivo [35S]methionine labeling of bundle-sheath strands isolated from light-grown leaves followed by immunoprecipitation revealed that bundlesheath strands synthesized plastidic [alpha]-amylase de novo.




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Copyright © 1995 by the American Society of Plant Biologists