| |
Software Requirements
Microsoft Internet Explorer 5.01 or higher and Netscape Navigator 4.75 or higher are recommended. |
|
 |
J.Health Sci., 57(1), 99-106, 2011
-Rapid Communication-
Characterization of a 62-Kilodalton Acidic Phospholipid-Binding Protein Isolated from the Edible Mushroom Pleurotus ostreatus
Hideko Tanaka and Tetsuyuki Kobayashi*
Department of Biological Sciences, Graduate School of Humanities and Sciences, Ochanomizu University, 2-1-1 Ohtsuka, Bunkyo-ku, Tokyo 112-8610, Japan
Many lipid-binding proteins such as pleurotolysin and ostreolysin have been isolated from the edible mushroom Pleurotus ostreatus. In this study, we detected a novel lipid-binding protein with a molecular weight of 62 kDa by measuring via centrifugation the association of aqueous extracts of the mushroom with lipid vesicles composed of various phospholipids. The 62-kDa protein (p62) was purified by sedimentation of the mixture of protein extracts and acidic phospholipid-containing lipid vesicles. The purified p62 bound to phosphatidylglycerol (PG)/phosphatidylcholine/cholesterol (5:45:50) vesicles but not to vesicles composed of other phospholipids including phosphatidylserine (PS), phosphatidylinositol, phosphatidic acid, lysoPS, and lysophosphatidylinositol. The p62 protein specifically associated with the PG-containing vesicles but not with other polyglycerophospholipid vesicles consisting of cardiolipin, bis(monoacylglycero)phosphate, monolysocardiolipin, or dilysocardiolipin, suggesting that p62 recognized a precise molecular structure of PG. Intrinsic tryptophan fluorescence of p62 was changed by incubation of p62 with PG-containing vesicles. Staining of giant unilamellar vesicles with fluorescence-labeled p62 showed that p62 bound to PG-containing vesicles but not PS-containing vesicles. These observations signify the potential usefulness of p62 as a tool for studying the functions of PG molecules in biological membranes.
|
|
