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LOCALIZATION OF AMYLOSE AND AN AMYLOSE‐BINDING LIPOPROTEIN IN NEUROSPORA CRASSA HYPHAE BY CYTOCHEMISTRY AND IMMUNOELECTRON MICROSCOPY
Author(s) -
VARKEY JACOB P.,
NADAKAVUKAREN MATHEW J.,
McCRACKEN DEREK A.
Publication year - 1985
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.1469-8137.1985.tb02868.x
Subject(s) - amylose , immunoelectron microscopy , neurospora crassa , biochemistry , chemistry , cytochemistry , hypha , staining , biology , biophysics , starch , botany , enzyme , antibody , gene , mutant , immunology , genetics
S ummary The presence of amylose was demonstrated in hyphal walls of Neurospora crassa Shen and Dodge by silver proteinate staining for carbohydrates and differential digestion with β‐amylase. The amylose was found to be localized in the innermost layer of the wall. Similarly, amylose‐precipitating factor (APF) was also found to be localized in the same wall layer using ferritin‐tagged antibodies to APF. Lipase‐digestion of the isolated hyphal wall resulted in considerable reduction of the silver grain deposition in the innermost wall layer, suggesting the removal of amylose from this layer. Because lipid‐free APF cannot bind to amylose, these observations indicate that APF and amylose in Neurospora are in a complexed form in the innermost layer of the hyphal wall as a structural component.