MODE OF TRYPTOPHAN RESIDUE ORIENTATION IN MYOSIN AND ACTION OF THE STRIATED MUSCLE FIBER

  • 1 January 1979
    • journal article
    • research article
    • Vol. 21  (2) , 171-+
Abstract
The mode of tryptophan residue orientation in myosin and actin myofilaments of the [rabbit] muscle fiber was studied using polarized UV fluorescent microscopy. During an extraction of protein from thick and thin myofilaments, changes in UV fluorescence anisotropy of muscle fibers were detected, suggesting that tryptophanil residues in myosin may be oriented parallel, but in actin perpendicular, to the muscle fiber axis. The use of acrylamide, a UV fluorescence quencher, is proposed for the control of extraction of proteins from muscle fibers.