Chemische Eigenschaften des mesodermalen Induktionsfaktors Verhalten bei der Zonenzentrifugierung

Abstract

A mesodermal inducing protein fraction isolated from chick embryos by ion-exchange-chromatography and electrophoresis was centrifuged in a sucrose-gradient for 72 hrs. It could thereby partially be separated into 2 components. The faster migrating component has the highest inducing activity. The amino acid composition of the 2 components is different. The molecular weight of the biologically active fraction could be estimated by comparison with the sedimentation velocity of protein of known molecular weight. Under the experimental conditions chosen (6m urea, ph 7.5) the molecular weight is of the order of 25.000-30.000.