Homogeneity among mitochondria revealed by a constant proportion of their enzymes.
The homogeneity or heterogeneity at the enzyme level of mitochondria has not been directly demonstrated and is important for many studies. To clarify this point, carbamoyl phosphate synthase (ammonia), glutamate dehydrogenase and mitochondrial adenosine triphosphatase (F1) were located in rat liver by immunolabeling using protein A-gold. Measurements of the number of gold particles per square micron of cross sectional images of mitochondria permit to assess the relative molecular concentration of the three enzymes and, most interestingly, it presents the first evidence that different mitochondria in rat liver cells have the same relative proportion of the three enzymes. Since they have vastly different half-lives, bulk or unregulated autophagy as the main mechanism regulating the turnover of these enzymes seems unlikely.
D000818:Animals; D002222:Carbamoyl-Phosphate Synthase (Ammonia) / Q000032:analysis; D005969:Glutamate Dehydrogenase / Q000032:analysis; D006046:Gold; D006207:Half-Life; D006651:Histocytochemistry; D007124:Immunoenzyme Techniques; D008297:Male; D008930:Mitochondria, Liver / Q000201:enzymology* / Q000648:ultrastructure; D006180:Proton-Translocating ATPases / Q000032:analysis; D051381:Rats; D011919:Rats, Inbred Strains; D013205:Staphylococcal Protein A
D013205:Staphylococcal Protein A; D006046:Gold; D005969:Glutamate Dehydrogenase; D006180:Proton-Translocating ATPases; D002222:Carbamoyl-Phosphate Synthase (Ammonia)