Secretion of acid phosphatase in Claviceps purpurea--an ultracytochemical study.
The lead phosphate precipitation method showed the reaction product of acid phosphatase (which reflects the presence of the enzyme glycoprotein) in peripheral cytoplasmic vesicles in the ascomycetous fungus Claviceps purpurea. The product appeared to diffuse from these vesicles (diameter 100-200 nm) towards the cell wall, usually to its sites covered by the capsular fibres exhibiting also acid phosphatase activity. This observation of diffusion of secretory glycoprotein in the cytoplasmic matrix and its orientation to the plasmalemma and capsular fibrils suggests an alternative to the well-described secretory mechanism of transport and exocytosis of glycoproteins via membrane-bound transport conveyors fusing with the cell membrane. It confirms and enlarges our previous finding of the reaction product of acid phosphatase performed by ultrastructural cytochemistry in vacuoles (lysosomes), in the growing cell septum, in cytoplasmic vesicles and in the fibres of the external capsule.
Vorísek
J
J
Institute of Microbiology, Academy of Sciences of the Czech Republic, 142 20 Prague, Czechia.
Kalachová
L
L
D000135:Acid Phosphatase / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002967:Claviceps / Q000201:enzymology* / Q000648:ultrastructure*; D003593:Cytoplasm / Q000378:metabolism; D022162:Cytoplasmic Vesicles / Q000201:enzymology / Q000648:ultrastructure; D004058:Diffusion; D008247:Lysosomes / Q000201:enzymology / Q000648:ultrastructure; D014617:Vacuoles / Q000201:enzymology / Q000648:ultrastructure
D000135:Acid Phosphatase