Abstract
Protein kinase activities were extracted from anther tissue of wheat (Triticum aestivum L. cv. Zaragoza) and characterized with regard to the effects of polyamines, second messengers and plant growth hormones. The protein kinases were inhibited by polyamines and cyclic nucleotides, but were stimulated by the addition of auxins, gibberellic acid and kinetin. The dominant polyamine-sensitive kinase activity was partially purified and characterized. The optimal pH of the reaction was 7.5 to 8.0 and casein was the preferred exogenous substrate. Polyamines were inhibiting in the decreasing order of putrecine > spermidine > spermine. The results are discussed against the context of the anther culture technique.
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