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Plant Physiology 100:756-761 (1992)
© 1992 American Society of Plant Biologists

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Cellular and Structural Biology

Purification of Maize Pollen Exines and Analysis of Associated Proteins 1

Christopher H. Chay, Erich G. Buehler, Judith M. Thorn, Thomas M. Whelan and Patricia A. Bedinger

Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599-3280

Zea mays (maize) pollen exines have been purified with the use of differential centrifugation and sucrose gradients, followed by mild detergent and high salt treatment. The final exine fraction is highly purified from other organelles and subcellular structures as assayed by transmission electron microscopy. Using mature maize pollen as the starting material, 0.2 to 0.3% of the total pollen protein remained associated with the exine fraction throughout the purification. Seven abundant sodium dodecyl sulfate-extractable proteins are detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the final fraction. Amino acid analysis reveals that one of the proteins contains a substantial amount of hydroxyproline, a characteristic of some primary cell wall proteins. The amino acid composition of the 25-kD protein strongly implies that it is an arabinogalactan protein. When exines are purified from earlier pollen developmental stages, a subset of the proteins found in the mature pollen exine is seen.

1 Supported by National Institutes of Health grant No. GM 38516, U.S. Department of Agriculture grant No. 91-37304-6656, and North Carolina Biotechnology Center grant No. 881010 to P.A.B., and a University of North Carolina Parent's Council grant to C.H.C.




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Copyright © 1992 by the American Society of Plant Biologists