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Location of SH-1 and SH-2 in the heavy chain segment of heavy meromyosin.
Authors:M Bálint  I Wolf  A Tarcsafalvi  J Gergely  F A Sréter
Institution:1. Department of Biochemistry, Eötvös Loránd University, H-1088 Budapest, Puskin u. 3, Hungary;2. Department of Muscle Research, Boston Biomedical Research Institute Boston, Massachusetts, USA;3. Departments of Biological Chemistry and Neurology, Harvard Medical School, and Massachusetts General Hospital, Boston, Massachusetts, USA
Abstract:The two essential thiol groups of myosin, SH-1 and SH-2, have been localized in an ~ 20K segment of the heavy chain by analysis of the distribution of radioactivity after tryptic digestion of tryptic heavy meromyosin (HMM) or papain-HMM subfragment-1, both labeled at SH-1 and SH-2 with 14C]iodoacetamide and 14C]N-ethyl maleimide, respectively. The results are discussed in the framework of earlier work (Bálint, M., Sréter, F. A., Wolf, I., Nagy, B., and Gergely, J. (1975) J. Biol. Chem. 250, 6168–6177) on the tryptic fragmentation of myosin heavy chain and in the light of more recent work on the location of a fragment that reacts with a photoaffinity analog of ATP (Szilágyi, L., Bálint, M., Sréter, F. A., and Gergely, J. (1978) Fed. Proc. 37, 1695) and of suggestions concerning the binding of ATP in the region containing the SH-1 and SH-2 (Elzinga, M., and Collins, J. H. (1977) Proc. Nat. Acad. Sci. USA74, 4281–4284).
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