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Tissue Distribution of Acetyl-Coenzyme A Carboxylase in Leaves ¹

Department of Biochemistry and Biophysics, University of California, Davis, California 95616

Acetyl-CoA carboxylase [acetyl-CoA—carbon dioxide ligase (ADP forming), EC 6.4.1.2] is a biotin-containing enzyme catalyzing the formation of malonyl-CoA. The tissue distribution of this enzyme was determined for leaves of C₃- and C₄-plants. The mesophyll tissues of the C₃-plants Pisum sativum and Allium porrum contained 90% of the leaf acetyl-CoA carboxylase activity, with the epidermal tissues containing the remainder. Western blotting of proteins fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, using ¹²⁵I-streptavidin as a probe, revealed biotinyl proteins of molecular weights 62,000, 51,000, and 32,000 in P. sativum and 62,000, 34,000, and 32,000 in A. porrum.

In the C₄-plant sorghum, epidermal protoplasts, mesophyll protoplasts and strands of bundle sheath cells contained 35, 47, and 17%, respectively, of the total leaf acetyl-CoA carboxylase activity. In Zea mays leaves the respective figures were 10% for epidermal protoplasts, 56% for mesophyll protoplasts, and 32% for bundle sheath strands. Biotinyl proteins of molecular weights 62,000 and 51,000 were identified in leaves of sorghum and Z. mays.

The results are discussed with respect to each tissue's requirements for malonyl-CoA for various metabolic pathways.

³ Present address: Native Plants, Inc., 417 Wakara Way, Salt Lake City, UT 84108.

¹ Supported in part by National Science Foundation Grants PCM79-03976 and PCM81-04497.

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