Cross-linking of phospholipids to proteins in the erythrocyte membrane |
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Authors: | G V Marinetti R Baumgarten D Sheeley S Gordesky |
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Affiliation: | Contribution from the Biochemistry Department The University of Rochester School of Medicine & Dentistry Rochester, New York 14642 USA |
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Abstract: | Erythrocytes treated with the cross-linking agents difluorodinitrobenzene and suberimidate are rendered refractory to lysis. When ghosts are treated with these reagents 8.4% and 2.3% of the total lipid phosphate is cross-linked to protein by difluorodinitrobenzene and suberimidate respectively. This represents 20 and 5.8% of the amino-phospholipids. The lipids extracted from treated ghosts do not react with ninhydrin as do lipids extracted from control ghosts. Thus essentially all the amino-phospholipids of the ghosts react with these cross-linking agents and up to 20% becomes cross-linked to proteins. |
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