Selective cleavage of the connector segments within the myosin-S1 heavy chain by staphylococcal protease.
The existence of the two connector segments linking the tryptic 50 kDa fragment of skeletal S1 heavy chain to the adjacent 27 kDa and 20 kDa peptides was ascertained by digestion of S1 with staphylococcal protease which was found to act specifically at these particular regions. Three new peptides of Mr 28000, 48000 and 22000 were produced and the novel S1 derivative formed had an intact actin-activated ATPase activity. Amino acid sequence analyses indicated that the 48 kDa and 22 kDa peptides overlap the two connector elements.
D000595:Amino Acid Sequence; D000818:Animals; D010450:Endopeptidases / Q000378:metabolism*; D007700:Kinetics; D008666:Metalloendopeptidases; D008970:Molecular Weight; D009132:Muscles; D015879:Myosin Subfragments; D009218:Myosins; D010446:Peptide Fragments / Q000032:analysis; D011817:Rabbits
D015879:Myosin Subfragments; D010446:Peptide Fragments; D010450:Endopeptidases; D008666:Metalloendopeptidases; C022653:auR protein, Staphylococcus aureus; D009218:Myosins