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Cambial cells of sycamore excrete a laccase-type polyphenol oxidase (EC 1.10.3.1 ) (Bligny and Douce, 1983). This type of enzyme, which utilizes molecular oxygen to oxidize phenolic substrates, is probably involved in lignin degradation processes (Mayer and Harel, 1979). This polyphenol oxidase is excreted by many mycorrhizal fungi (for a review, see Mayer, 1987) and is present in some higher plant cells including the genus Rhus (Rhus vernicifera, see Reinhammar, 1970), Aesculus (Wosilait et aG, 1954) and Prunus (Lehman et al., 1974). The enzyme was purified from the nutrient medium, into which it was excreted by suspension-cultured sycamore cells, using classical purification techniques including a concanavalin A-Sepharose affinity column. The sycamore cell laccase is a monomeric blue copper protein containing 45% carbohydrate and 4 copper atoms (one type 1 and 2 CU2+ and two type 3 Cu 2+) per molecule. The molecular mass (M r = 97 000) was calculated from the sedimen-

Excretion of laccase by sycamore (Acer pseudoplatanus L.) cambial cells: effect of copper deficiency, reversible removal of type 2 Cu2+

Excretion of laccase by sycamore (Acer pseudoplatanus L.) cambial cells: effect of copper deficiency, reversible removal of type 2 Cu²⁺