Morphogenesis of Agaricus bisporus: Changes in Proteins and Enzyme Activity

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Abstract
Soluble proteins from various tissues of the different morphogenetic stages of A. bisporus were analyzed qualitatively and quantitatively. In 2 of the 3 commercial strains studied the soluble-protein content of the caps was significantly higher than in the other tissues. The protein profiles of the caps, stalks, pins or primordia and the mycelium were different when studied by polyacrylamide-gel electrophoresis. Cytochrome oxidase and tyrosinase activities were highest in the pins and lowest in the tissues of the cap. The isozyme-banding patterns of cytochrome oxidase and peroxidase varied in the tissue extracts of the different morphogenetic stages. Zymograms of cytochrome oxidase were similar in cap, pin and stalk extracts. However, 2 of these bands were lacking in the mycelial extracts. Gels stained for peroxidase showed the largest number of bands in the mycelial extracts. The role of these enzymes in morphogenesis of the mycelium to the primordium and finally to the mushroom is discussed.