Effect of crosslinking on mitochondrial structure and function.
Rat liver mitochondria were treated with ethylacetimidate and methylbutyrimidate, monofunctional imidates, and with dimethylsuberimidate, a bifunctional imidate, and the effects on structure and function studied. Mitochondria treated with 5 mM dimethylsuberimidate or greater did not respond osmotically when placed in deionized water. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed that at concentrations greater than 5 mM dimethylsuberimidate nearly all mitochondrial polypeptides failed to enter 6% gels, indicating crosslinking of both membrane and soluble proteins. Extensive amidination by ethylacetimidate and methylbutyrimidate had little effect on ascorbate-tetramethylphenylenediamine oxidase while extensive inhibition resulted from dimethylsuberimidate treatment. The possible involvement of molecular motion in electron transport is discussed.
D000477:Alkylating Agents; D000586:Amination; D000818:Animals; D001204:Ascorbate Oxidase / Q000378:metabolism; D003864:Depression, Chemical; D004120:Dimethyl Suberimidate / Q000494:pharmacology; D004579:Electron Transport / Q000187:drug effects; D007094:Imides / Q000494:pharmacology*; D008566:Membranes / Q000187:drug effects; D008930:Mitochondria, Liver / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D009996:Osmotic Fragility / Q000187:drug effects; D011506:Proteins / Q000378:metabolism; D051381:Rats
D000477:Alkylating Agents; D007094:Imides; D011506:Proteins; D004120:Dimethyl Suberimidate; D001204:Ascorbate Oxidase