The importance of the mitochondrial protein synthesizing system in the development of functional mitochondria, and thus presumably in the pathogenesis of mitochondrial cytopathies has become apparent in recent years. A procedure has been developed to allow the measurement of the protein synthetic activity in mitochondria isolated from human skeletal muscle biopsy materials. The examination of the mitochondrial protein synthesis products revealed two polymorphic variants with the electrophoretic mobilities in SDS-polyacrylamide gel of a 20/22 kDa and a 45/47 kDa protein. Since functional consideration suggests that these variants are most likely to be associated with conservative amino acid substitutions, the observation indicates that it might be possible to electrophoretically detect certain alterations in the mitochondrial translation products in mitochondrial cytopathies due to mutations in the mitochondrial genome.