Interaction of studies of a 100,000 dalton chymotryptic fragment of rabbit skeletal M-line protein with the S2 subfragment of myosin.
Controlled chymotryptic digestion of the 165,000 dalton component of the M-line of rabbit skeletal muscle, followed by Biogel P-150 chromatography of the digest, has led to the isolation of a homogeneous 100,000 dalton species. This fragment was found, by both sedimentation equilibrium and gel filtration chromatography, to interact with heavy meromyosin subfragment 2 (HMM-S2). The persistence of this fragment, after chymotryptic digestion, to bind HMM-S2, along with the known insensitivity of the M-line to proteolysis, suggests a structural role for the parent 165,000 dalton component along the lines of the M-filament, as suggested by the Knappeis and Carlsen model for M-line structure.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002918:Chymotrypsin; D008970:Molecular Weight; D009124:Muscle Proteins; D009132:Muscles / Q000032:analysis*; D009218:Myosins; D010446:Peptide Fragments; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits
D000596:Amino Acids; D009124:Muscle Proteins; D010446:Peptide Fragments; D002918:Chymotrypsin; D009218:Myosins