Abstract
Shoot apex proteins from 11 seedlings, two juvenile clones and three mature grafted clones of Sequoiadendron giganteum (Lindl.) Buchh. were examined throughout the year by SDS-polyacrylamide gel electrophoresis. A membrane-associated protein known as J 16, with an approximate molecular weight of 16 kD, was always detected in juvenile tissue, but was absent in tissue of the mature clones. The J 16 protein was also present in extracts of a mature clone that had been morphologically rejuvenated by micrografting. Protein extracts from the rejuvenated clone, were separated by electrophoresis and assayed for J 16 using an immunoblotting procedure with anti-J 16 serum. This test revealed two bands, J 16 and another protein with a lower molecular weight. The small molecular weight protein was not detected in juvenile clones.

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