Abstract
Proteolytic digestion of the M-protein of Sendai virus produces a product with a mol. wt. approximately 5000 less than that of the intact protein. In the case of digestion with chymotrypsin this cleavage is quite specific and the cleaved protein can be isolated. The smaller fragment appears to be physically removed from the larger (30000 mol. wt.) fragment, rather than remaining in non-covalent association with it. The cleavage is likely to be near the N-terminus of the protein. At the present time there is no indication of the biological function of this fragment.
* Present and reprint address: Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW.
† Present address: Max Planck-Institut für Molecular Genetik, Ihrestrasse 6373, 1 Berlin 33 (Dahlen), W. Germany.