Light and Electron Microscopical Localization of Lysosomal Acid Hydrolases in Bivalve Haemocytes by Enzyme Cytochemistry.

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  • Cajaraville Miren P.
    Biologia Zelularra eta Zientzia Morfologikoen Saila, Euskal Herriko Unibertsitatea/Universidad del País Vasco
  • Pal Santi G.
    Biologia Zelularra eta Zientzia Morfologikoen Saila, Euskal Herriko Unibertsitatea/Universidad del País Vasco Present address: Calcutta University, Department of Zoology
  • Robledo Yolandr
    Biologia Zelularra eta Zientzia Morfologikoen Saila, Euskal Herriko Unibertsitatea/Universidad del País Vasco

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In the present work the haemocytes of mussels Mytilus galloprovincialis (Mollusca, Bivalvia) have been studied by enzyme cytochemistry in order to investigate the light and electron microscopical distribution of two lysosomal marker enzymes, acid phosphatase (AcPase) and arylsulphatase (ASase). Both hyalinocytes and granulocytes show positive reaction products for the two enzymes but granulocytes are far more reactive. In the hyalinocytes, AcPase and ASase activities are observed in a few pleomorphic lysosomes. In the granulocytes, the reaction product for the enzymes is found in Golgi bodies; AcPase is restricted to small trans-Golgi vesicles while ASase is localized in all the cisterns and vesicles. In addition, some but not all specific granules show both AcPase and ASase activities, mostly associated to their periphery. These results confirm that the granules of mussel granulocytes, although apparently similar in morphology, are functionally heterogeneous with regard to enzyme composition. Cortical or peripheral vesicular organelles are negative for AcPase but some are positive for ASase, indicating their endolysosomal nature. Larger vesicles containing remnants of algal cells do show strong AcPase activity and are thus considered as phagolysosomes. In controls incubated without substrates no precipitation of reaction products was detected either for AcPase nor for ASase.

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