Work

Myogenic growth factor present in skeletal muscle is purified by heparin-affinity chromatography.

Year: 1985

Type: article

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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.82.23.8044

Authors: E Kardami, D Spector, R C Strohman

Institution: University of California, Berkeley

Language: English

Topic: Muscle Physiology and Disorders

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: Muscular Dystrophy Association, National Institutes of Health

OpenAlex ID: W1966686134

FWCI: 2.626

Cites: 29

Cited by: 84

Related to: 10