Tissue fixation by osmium tetroxide. A possible role for proteins.

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Abstract
The osmiophilia, under the conditions of normal tissue fixation, of the histidine, lysine, tryptophan, cysteine and methionine side chain of proteins is suggested by in vitro studies on blocked amino acids representative of such protein side chains, and the chemical nature of the reaction products elucidated. The chemical feasibility of inter- or intramolecular cross-linking of protein by OsO4 at these and other sites is demonstrated, as in the cross-linking of protein with unsaturated lipids such as methyl oleate, methyl linoleate and linolenate, and cholesteryl acetate. The relevance of these results to the process of tissue fixation by OsO4 is discussed.