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Localizing an Ophiostoma piceae proteinase in sapwood of four tree species using polyclonal antibodies
Author(s) -
GHARIBIAN S.,
HOFFERT C.,
ABRAHAM L. D.,
BREUIL C.
Publication year - 1996
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.1469-8137.1996.tb01936.x
Subject(s) - pinus contorta , tsuga , botany , biology , polyclonal antibodies , fungus , western hemlock , ophiostoma , proteolytic enzymes , enzyme , antibody , biochemistry , immunology
summary The growth and proteolytic activity of the sap‐staining fungus Ophiostoma piceae were characterized in the wood of four tree species: lodgepole pine ( Pinus contorta var. latifolia Dougl.), aspen ( Populus tremuloides Michx.), Douglas fir ( Pseudotsuga menziesii (Mirb.) Franco) and Western hemlock ( Tsuga heterophylla Sarg.). Proteolytic activity and growth were highest in aspen. Proteolytic activity was minimal in both Douglas fir and Western hemlock. Polyclonal antibodies raised against the major proteinase produced by O. picaea were used to immunolocalize the enzyme after fungal growth in lodgepole pine and aspen. Immunogold labelling revealed that the proteinase was localized mainly in the cell wall of O. piceae. Gold particles concentrated in a sheath which was well defined after 10 d. Labelling appeared greater in the inoculated aspen than in lodgepole pine.