Release of Spectrin-Containing Vesicles from Human Erythrocyte Ghosts by Dimyristoylphosphatidylcholine^1
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- YAMAGUCHI Takeo
- Department of Chemistry, Faculty of Science, Fukuoka University
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- YAMAMOTO Misuzu
- Department of Chemistry, Faculty of Science, Fukuoka University
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- KIMOTO Eiji
- Department of Chemistry, Faculty of Science, Fukuoka University
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抄録
Membrane vesicles, which were released from human erythrocyte ghosts by dimyristoylphosphatidylcholine (DMPC), showed a protein composition similar to that of the erythrocyte membrane, despite a reduction of in spectrin content. The spectrin content of vesicles decreased with increasing hemoglobin concentration within ghost membranes, but increased upon exposure of hemoglobin-free ghosts to a pressure of 100 MPa. The ESR spectra of spin-labeled membrane proteins showed that membrane proteins in ghosts became unfolded at high pressure. Furthermore, spectrin-poor and protein 4.1-rich vesicles were released by DMPC from diamide-treated ghosts in which spectrin was cross-linked and stabilized. Taking into account that the spectrin tetramer is stabilized by hemoglobin [Liu and Palek (1984) J. Biol. Chem. 259, 11556-11562], these results suggest that the spectrin content of DMPC-induced vesicles from erythrocyte ghosts increases with increasing instability of the cytoskeletal network in parent cells.
収録刊行物
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- The journal of biochemistry
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The journal of biochemistry 119 (1), 95-99, 1996-01-01
社団法人 日本生化学会
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詳細情報 詳細情報について
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- CRID
- 1571417124331638144
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- NII論文ID
- 10005185112
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- NII書誌ID
- AA00694073
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- ISSN
- 0021924X
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- 本文言語コード
- en
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- データソース種別
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- CiNii Articles