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Electrophoretic and immunological studies on acid phosphatase from a mycorrhizal fungus of Erica hispidula L.
Author(s) -
STRAKER C. J.,
GIANINAZZIPEARSON VIVIENNE,
GIANINAZZI S.,
CLEYETMAREL J.C.,
BOUSQUET N.
Publication year - 1989
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/j.1469-8137.1989.tb00685.x
Subject(s) - immunogold labelling , acid phosphatase , antiserum , biology , hypha , phosphatase , fungus , concanavalin a , collodion , cytoplasm , cytochemistry , glycoprotein , biochemistry , ultrastructure , botany , mycorrhiza , microbiology and biotechnology , antigen , membrane , symbiosis , enzyme , bacteria , immunology , genetics , in vitro
summary Wall‐bound acid phosphatases of an endomycorrhizal fungus of Erica hispidula L. were separated by PAGE, electrotransferred to nitrocellulose membranes and glycoprotein characteristics studied using Concanavalin A. An antiserum was raised against the major high‐molecular‐weight acid phosphatase and its specificity demonstrated by immunoblotting and ELISA. The antiserum reacted very little with protein extracts of other cellular fractions and was unable to bind to wall‐bound protein antigens of a mycorrhizal isolate from K. mauritanica. Ultrastructural localization of acid phosphatase by cytoenzymology and indirect immunogold labelling showed it to be almost exclusively associated with the fungal wall and septa of living hyphae, whilst in senescent hyphae it was also present within the disorganized cytoplasm.