Products of rat liver mitochondrial protein synthesis: Electrophoretic analysis of the number and size of these proteins and their solubility in chloroform: Methanol

1974 ◽  
Vol 164 (1) ◽  
pp. 1-11 ◽  
Author(s):  
James P. Burke ◽  
Diana S. Beattie
Keyword(s):  
Protein Synthesis ◽  
Rat Liver ◽  
Mitochondrial Protein ◽  
Electrophoretic Analysis ◽  
Mitochondrial Protein Synthesis ◽  
Chloroform Methanol

Effect of rifampicin on mitochondrial protein synthesis in rat liver

1973 ◽  
Vol 22 (5) ◽  
pp. 659-660 ◽  
Author(s):  
Dipak K. Dube ◽  
Syamalima Chakrabarti ◽  
Aditi Sarkar ◽  
Prabir. Bhattacharya ◽  
Bishendu B. Goswami ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Rat Liver ◽  
Mitochondrial Protein ◽  
Mitochondrial Protein Synthesis

Products of mitochondrial protein synthesis in Tetrahymena

1979 ◽  
Vol 57 (4) ◽  
pp. 314-320 ◽  
Author(s):  
Paul G. Young ◽  
Neil P. Hunter
Keyword(s):  
Protein Synthesis ◽  
Gel Electrophoresis ◽  
Trichloroacetic Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Mitochondrial Protein ◽  
Sodium Dodecyl ◽  
Apparent Molecular Weight ◽  
Mitochondrial Proteins ◽  
Mitochondrial Protein Synthesis ◽  
Chloroform Methanol

The products of mitochondrial protein synthesis have been investigated in Tetrahymena after labelling with [35S]methionine in the presence of cycloheximide. The labelled proteins were analyzed by sodium dodecyl sulfate slab polyacrylamide gel electrophoresis. We have identified 13 electrophoretically discrete bands as well as 4 other bands with a more variable occurrence. These proteins ranged in apparent molecular weight from 8100 to 57 500. The cycloheximide-resistant incorporation could be blocked with chloramphenicol. The mitochondrial proteins appeared to be in a disaggregated state and were stable to agents such as trichloroacetic acid (hot or cold) and chloroform–methanol. The pattern of proteins was similar following labelling times ranging from 30 min to 3 h.

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