Studies on the possible occurrence of actomyosin-like proteins in phloem.

Extracts of large quantities of petioles and of isolated vascular tissues of Heracleum mantegazzianum have been analysed for actomyosin-like contractile proteins. Concentrated preparations, subjected to a standard isolation and purification procedure for actomyosin, failed to demonstrate either superprecipitation or viscosity changes in response to the addition of ATP and divalent cations. In addition, ATPase activities in phloem and xylem extracts have been fractionated by gel electrophoresis and characterised with regard to their substrate specificity, pH optima and ion requirements. Phloem extracts provide two phosphatases: one is non-specific in its substrate requirements; the other is a nucleoside triphosphatase but is stimulated only by monovalent cations and is also present in xylem extracts. All the enzymes are strongly inhibited by divalent cations and do not possess any of the characteristics of ATPases associated with contractile systems. The results are discussed in relation to the postulated involvement of contractile proteins in the translocation of sugars in phloem.