Protein synthesis in mitochondria. 3. The controlled disruption and subfractionation of mitochondria labelled <i>in vitro</i> with radioactive valine

DB ROODYN

Biochemical Journal · 1962 · 127 citations · 20 references

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Abstract

The aldolas3 concentration in sarcoplasm from foetal skeletal muscle is low, like that of adult heart muscle, although the enzymic activity rises as the foetus develops. The general conclusion of this comparison is that at least for the components moving towards the cathode foetal-muscle sarco- plasm is more comparable with that of adult heart muscle than that of white skeletal muscle. The sarcoplasm of red skeletal muscle appears to be intermediate between these two types. The high concentration of aldolase in the adult-skeletal- muscle sarcoplasm might be expected in view of the well-developed ability of this tissue to function anaerobically. These facts together with our find- ings suggest that after birth aldolase and other proteins of a high isoelectric point increase rapidly in amount in response to the increased activity of the skeletal muscle. SUMMARY 1. Rabbit skeletal muscle has been fractionated by chromatography on diethylaminoethylcellulose at pH 7-6 and 9-3.

References

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