Alteration of the conformation of proteins in red blood cell membranes and in solution by fixatives used in electron microscopy.
The effects of several commonly employed fixatives on the three-dimensional conformations of two soluble proteins and the protein of intact red blood cell membranes have been studied by means of circular dichroism measurements in the spectral region of the peptide absorption bands. The fixatives used produced significant and parallel conformational changes in all of the proteins, in the increasing order: glutaraldehyde; OsO(4); glutaraldehyde followed by OsO(4); and KMnO(4). The last two treatments obliterated most of the helical character of the proteins. The significance of these observations to the preparation of specimens for electron microscopy is discussed.
D000818:Animals; D002417:Cattle; D002462:Cell Membrane / Q000187:drug effects*; D055598:Chemical Phenomena; D002621:Chemistry; D004912:Erythrocytes / Q000166:cytology / Q000187:drug effects; D006801:Humans; D007202:Indicators and Reagents / Q000494:pharmacology*; D008322:Mammals; D008854:Microscopy, Electron; D011506:Proteins / Q000032:analysis*; D012709:Serum Albumin / Q000032:analysis
D007202:Indicators and Reagents; D011506:Proteins; D012709:Serum Albumin