Abstract
The combined low-molecular-weight protein components of the myogens from carp white and red muscles [about 30% (w/w) of the myogen proteins] have been isolated by gel filtration on Sephadex G-75 columns. The presence in this fraction from myogen of white muscle of the three main electro-phoretic components previously isolated has been confirmed, and the low molecular weight of the fourth component has been definitely established. The exclusive presence of this fourth component in the myogen of red muscle, apart from myoglobin, has also been demonstrated. Glycogenolysis experiments in vitro have shown that the low-molecular-weight protein fraction from carp myogen does not contain enzymes from the Embden-Meyerhof chain.