Isolation and partial characterization of a carbohydrate-binding protein from a nematode-trapping fungus.
A developmentally regulated carbohydrate-binding protein from the capture organs of Arthrobotrys oligospora, not present on hyphae, was isolated and partially characterized. Surface structures of A. oligospora were radiolabeled with [125I]iodosulfanilic acid. The fungus was homogenized, and the homogenate was passed over an affinity column containing N-acetyl-D-galactosamine immobilized to Sepharose 6B. The bound radiolabeled protein was eluted from the affinity column with a glycine-hydrochloride buffer (pH 3.0), concentrated, and chromatographed on a metal chelate affinity gel containing Ca2+. EDTA was used as an eluant for the radiolabeled protein. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis in combination with autoradiography revealed a molecular weight for the carbohydrate- and cation-binding polypeptide of ca. 20,000.
D000116:Acetylgalactosamine / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D005656:Fungal Proteins; D005688:Galactosamine / Q000031:analogs & derivatives*; D007457:Iodine Radioisotopes; D037102:Lectins; D003904:Mitosporic Fungi / Q000378:metabolism*; D008970:Molecular Weight; D009348:Nematoda; D013425:Sulfanilic Acids
D002352:Carrier Proteins; D005656:Fungal Proteins; D007457:Iodine Radioisotopes; D037102:Lectins; D013425:Sulfanilic Acids; C041890:carbohydrate-binding protein, nematophagous fungi; D005688:Galactosamine; D000116:Acetylgalactosamine