Characterization of a 62-Kilodalton Acidic Phospholipid-Binding Protein Isolated from the Edible Mushroom Pleurotus ostreatus
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- Tanaka Hideko
- Department of Biological Sciences, Graduate School of Humanities and Sciences, Ochanomizu University
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- Kobayashi Tetsuyuki
- Department of Biological Sciences, Graduate School of Humanities and Sciences, Ochanomizu University
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Abstract
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.
Journal
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- Journal of Health Science
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Journal of Health Science 57 (1), 99-106, 2011
The Pharmaceutical Society of Japan
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Details 詳細情報について
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- CRID
- 1390001204497794816
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- NII Article ID
- 130000425130
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- NII Book ID
- AA11316464
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- ISSN
- 13475207
- 13449702
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- NDL BIB ID
- 10952043
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed