Properties of amino acid composition of the tryptic fragments of the heavy chain of myosin subfragment-1.
Limited tryptic digestion of the heavy chain of chymotryptic myosin subfragment-1 gives three major fragments with approximate molecular weights of 50 K, 27 K, and 20 K daltons. We previously reported (Hozumi, T. & Muhlrad, A. (1981) Biochemistry 20, 2945-2950) that these fragments can be separated by gel filtration in 1% sodium dodecyl sulfate. By using this method, the tryptophan content and amino acid composition of fragments were measured. The 27 K and 50 K fragments were found to be rich in tryptophan, in contrast to the 20 K fragment.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D015879:Myosin Subfragments; D009218:Myosins / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis*; D011817:Rabbits; D014357:Trypsin / Q000378:metabolism*; D014364:Tryptophan / Q000032:analysis
D000596:Amino Acids; D015879:Myosin Subfragments; D010446:Peptide Fragments; D014364:Tryptophan; D014357:Trypsin; D009218:Myosins