Abstract
Summary Dry, quiescent gametophyte cells of Welwitschia mirabilis seed contain approximately 25 % protein and 30 % fat. Cytochemical localization of protein and carbohydrate at the light and electron microscope levels indicates that the stored reserves of the protein body as a whole exist as a protein-carbohydrate complex. Upon imbibition protein hydrolysis precedes lipid digestion, and decrease in protein during germination is concurrent with a loss of electron-dense granular material from protein body matrices. Proteolytic enzymes are transported by ER-derived vesicles that enter the protein body and stain positively for acid phosphatase. Protein body globoids in both gametophyte and embryo feeder cells are characteristically associated with acid phosphatase activity. Acid phosphatase activity is also found associated with the amorphous eccentric cores of the microbodies of gametophyte and feeder cells, but not all microbodies show a positive reaction. Acid phosphatase is also localized in lipid bodies of feeder cells as well as in senescing feeder interface cells, but not in those of the gametophyte. During senescence of feeder interface cells acid phosphatase is intensely localized in the region of degradation of the middle lamella.
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