Controlled proteolytic digestion of the M-protein of Sendai virus: the isolation of a fragment of 30000 molecular weight.
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.
D000596:Amino Acids / Q000032:analysis; D002918:Chymotrypsin / Q000378:metabolism; D008970:Molecular Weight; D010222:Parainfluenza Virus 1, Human / Q000032:analysis* / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism; D014764:Viral Proteins / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism
D000596:Amino Acids; D014764:Viral Proteins; D002918:Chymotrypsin; D014357:Trypsin