Myogenic growth factor present in skeletal muscle is purified by heparin-affinity chromatography.
- 1 December 1985
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 82 (23) , 8044-8047
- https://doi.org/10.1073/pnas.82.23.8044
Abstract
A myogenic growth factor has been purified from a skeletal muscle, the anterior latissimus dorsi, of adult chickens. In the range of 1-10 ng, this factor stimulates DNA synthesis as well as protein and muscle-specific myosin accumulation in myogenic cell cultures. Purification is achieved through binding of the factor to heparin. The factor is distinct from transferrin and works synergistically with transferrin in stimulating myogenesis in vitro.This publication has 27 references indexed in Scilit:
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