Photocross-linking from DNPated SH1 in myosin head. I. Cross-linking to the 50-kDa fragment.

@article{Muno1987PhotocrosslinkingFD,
  title={Photocross-linking from DNPated SH1 in myosin head. I. Cross-linking to the 50-kDa fragment.},
  author={D. Muno and N. Sutoh and T. Sekine},
  journal={Journal of biochemistry},
  year={1987},
  volume={101 3},
  pages={
          661-9
        }
}
When DNP-SH1-myosin, selectively dinitrophenylated at SH1 by 1,2,4-trinitrobenzene, was irradiated with a high-pressure mercury lamp equipped with a UV cut filter, a new 220-kDa band called the X-band appeared right above the heavy chain band (200 kDa) on SDS-PAGE (Laemmli). The time course of the X-band formation was composed of two phases, the initial one being rapid, and the second slow. Immune reaction experiments using antibodies specific for heavy or light chains indicated that the X-band… Expand
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Glutamic acid-88 is close to SH-1 in the tertiary structure of myosin subfragment 1.
TLDR
Peptides containing cross-links were isolated by liquid chromatography and subjected to amino acid sequence analyses and show that Glu-88 is the major site and Asp-89 and Met-92 are the minor sites involved in cross-linking with SH-1 (Cys-707) via BPIA. Expand
Pathway for the communication between the ATPase and actin sites in myosin
S-1 EDC K ATP LC~ LC3 EDTA DTNB EEDQ IAEDANS TNBS DTE IAA FDNB NEM pPDM Bz2-ATP NPIA TNB DHNBS BPIA FNBD MANTP MANDP DNP BMBP myosin subfragment-1 1-ethyl-3(3-dimethylamino propyl) carbodiimideExpand