메뉴 건너뛰기




Volumn 74, Issue 6, 1998, Pages 3083-3092

Steady-state fluorescence polarization studies of the orientation of myosin regulatory light chains in single skeletal muscle fibers using pure isomers of iodoacetamidotetramethylrhodamine

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN;

EID: 0031806116     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)78015-4     Document Type: Article
Times cited : (38)

References (39)
  • 1
    • 0026985623 scopus 로고
    • Stereospecific reaction of muscle fiber proteins with the 5′ or 6′ isomer of (iodoacetamido)tetramethylrhodamine
    • Ajtai, K., P. J. K. Ilich, A. Ringler, S. S. Sedarous, D. J. Toft, and T. P. Burghardt. 1992. Stereospecific reaction of muscle fiber proteins with the 5′ or 6′ isomer of (iodoacetamido)tetramethylrhodamine. Biochemistry. 31:12431-12440.
    • (1992) Biochemistry , vol.31 , pp. 12431-12440
    • Ajtai, K.1    Ilich, P.J.K.2    Ringler, A.3    Sedarous, S.S.4    Toft, D.J.5    Burghardt, T.P.6
  • 2
    • 0029975892 scopus 로고    scopus 로고
    • Orientation changes in myosin regulatory light chains following photorelease of ATP in skinned muscle fibers
    • Allen, T. StC., N. Ling, M. Irving, and Y. E. Goldman. 1996. Orientation changes in myosin regulatory light chains following photorelease of ATP in skinned muscle fibers. Biophys. J. 70:1847-1862.
    • (1996) Biophys. J. , vol.70 , pp. 1847-1862
    • Allen, T.StC.1    Ling, N.2    Irving, M.3    Goldman, Y.E.4
  • 3
    • 0029774205 scopus 로고    scopus 로고
    • Fluorescence polarization of skeletal muscle fibers labeled with rhodamine isomers on the myosin heavy chain
    • Berger, C. L., J. S. Craik, D. R. Trentham, J. E. T. Corrie, and Y. E. Goldman. 1996. Fluorescence polarization of skeletal muscle fibers labeled with rhodamine isomers on the myosin heavy chain. Biophys. J. 71:3330-3343.
    • (1996) Biophys. J. , vol.71 , pp. 3330-3343
    • Berger, C.L.1    Craik, J.S.2    Trentham, D.R.3    Corrie, J.E.T.4    Goldman, Y.E.5
  • 5
    • 0021014578 scopus 로고
    • Evidence for crossbridge order in contraction of glycerinated skeletal muscle
    • Burghardt, T. P., T. Ando, and J. Borejdo. 1983. Evidence for crossbridge order in contraction of glycerinated skeletal muscle. Proc. Natl. Acad. Sci. USA. 80:7515-7519.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 7515-7519
    • Burghardt, T.P.1    Ando, T.2    Borejdo, J.3
  • 6
    • 0000315888 scopus 로고
    • Fluorescence polarization: Measurement with ultraviolet polarizing filters in a spectrophotofluorimeter
    • Chen, R. F., and R. L. Bowman. 1965. Fluorescence polarization: measurement with ultraviolet polarizing filters in a spectrophotofluorimeter. Science. 147:729-732.
    • (1965) Science , vol.147 , pp. 729-732
    • Chen, R.F.1    Bowman, R.L.2
  • 7
    • 0020425131 scopus 로고
    • Orientation of spin labels attached to cross-bridges in contracting muscle fibers
    • Cooke, R., M. S. Crowder, and D. D. Thomas. 1982. Orientation of spin labels attached to cross-bridges in contracting muscle fibers. Nature. 300:776-778.
    • (1982) Nature , vol.300 , pp. 776-778
    • Cooke, R.1    Crowder, M.S.2    Thomas, D.D.3
  • 9
    • 37049075338 scopus 로고
    • Synthesis and characterisation of pure isomers of iodoacetamidotetramethylrhodamine
    • Corrie, J. E. T., and J. S. Craik. 1994. Synthesis and characterisation of pure isomers of iodoacetamidotetramethylrhodamine. J. Chem. Soc., Perkin Trans. 1. 2967-2974.
    • (1994) J. Chem. Soc., Perkin Trans. 1 , pp. 2967-2974
    • Corrie, J.E.T.1    Craik, J.S.2
  • 10
    • 0018816862 scopus 로고
    • The relation of muscle biochemistry to muscle physiology
    • Eisenberg, E., and L. E. Greene. 1980. The relation of muscle biochemistry to muscle physiology. Annu. Rev. Physiol. 42:293-309.
    • (1980) Annu. Rev. Physiol. , vol.42 , pp. 293-309
    • Eisenberg, E.1    Greene, L.E.2
  • 11
    • 0021992946 scopus 로고
    • Muscular contraction and free energy transduction in biological systems
    • Eisenberg, E., and T. L. Hill. 1985. Muscular contraction and free energy transduction in biological systems. Science. 227:999-1006.
    • (1985) Science , vol.227 , pp. 999-1006
    • Eisenberg, E.1    Hill, T.L.2
  • 12
    • 0025989807 scopus 로고
    • Orientational disorder and motion of weakly attached cross-bridges
    • Fajer, P. G., E. A. Fajer, M. Schoenberg, and D. D. Thomas. 1991. Orientational disorder and motion of weakly attached cross-bridges. Biophys. J. 60:642-649.
    • (1991) Biophys. J. , vol.60 , pp. 642-649
    • Fajer, P.G.1    Fajer, E.A.2    Schoenberg, M.3    Thomas, D.D.4
  • 13
    • 85030335617 scopus 로고    scopus 로고
    • Effects of temperature and ionic strength on myosin head orientation in relaxed demembranated fibers from rabbit psoas muscle, studied with a birefringence-interference microscope
    • Folkes, D. E., N. C. Millar, and M. Irving. 1996. Effects of temperature and ionic strength on myosin head orientation in relaxed demembranated fibers from rabbit psoas muscle, studied with a birefringence-interference microscope. Biophys. J. 70:A17.
    • (1996) Biophys. J. , vol.70
    • Folkes, D.E.1    Millar, N.C.2    Irving, M.3
  • 14
    • 0021287261 scopus 로고
    • Control of sarcomere length in skinned muscle fibers of Rana temporaria during mechanical transients
    • Goldman, Y. E., and R. M. Simmons. 1984. Control of sarcomere length in skinned muscle fibers of Rana temporaria during mechanical transients. J. Physiol. (Lond.). 350:497-518.
    • (1984) J. Physiol. (Lond.) , vol.350 , pp. 497-518
    • Goldman, Y.E.1    Simmons, R.M.2
  • 15
    • 0026061117 scopus 로고
    • Orientation of spin-labeled light chain-2 exchanged into myosin crossbridges in glycerinated muscle fibers
    • Hambly, B., K. Franks, and R. Cooke. 1991. Orientation of spin-labeled light chain-2 exchanged into myosin crossbridges in glycerinated muscle fibers. Biophys. J. 59:127-138.
    • (1991) Biophys. J. , vol.59 , pp. 127-138
    • Hambly, B.1    Franks, K.2    Cooke, R.3
  • 16
    • 0026619792 scopus 로고
    • Paramagnetic spin probes attached to a light chain on the myosin head are highly disordered in active muscle fibers
    • Hambly, B., K. Franks, and R. Cooke. 1992. Paramagnetic spin probes attached to a light chain on the myosin head are highly disordered in active muscle fibers. Biophys. J. 63:1306-1313.
    • (1992) Biophys. J. , vol.63 , pp. 1306-1313
    • Hambly, B.1    Franks, K.2    Cooke, R.3
  • 17
    • 0031079847 scopus 로고    scopus 로고
    • The swinging lever arm hypothesis of muscle contraction
    • Holmes, K. C. 1997. The swinging lever arm hypothesis of muscle contraction. Curr. Biol. 7:R112-R118.
    • (1997) Curr. Biol. , vol.7
    • Holmes, K.C.1
  • 19
    • 0031806323 scopus 로고    scopus 로고
    • Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers
    • Hopkins, S. C., C. Sabido-David, J. E. T. Corrie, M. Irving, and Y. E. Goldman. 1998. Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers. Biophys. J. 74:3093-3110.
    • (1998) Biophys. J. , vol.74 , pp. 3093-3110
    • Hopkins, S.C.1    Sabido-David, C.2    Corrie, J.E.T.3    Irving, M.4    Goldman, Y.E.5
  • 20
    • 0029961637 scopus 로고    scopus 로고
    • Steady state polarization from cylindrically-symmetric fluorophores undergoing rapid restricted motion
    • Irving, M. 1996. Steady state polarization from cylindrically-symmetric fluorophores undergoing rapid restricted motion. Biophys. J. 70: 1830-1835.
    • (1996) Biophys. J. , vol.70 , pp. 1830-1835
    • Irving, M.1
  • 22
    • 0027446431 scopus 로고
    • The effect of lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers, 1. Proportionality between the lattice spacing and the fiber width
    • Kawai, M., J. S. Wray, and Y. Zhao. 1993. The effect of lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers, 1. Proportionality between the lattice spacing and the fiber width. Biophys. J. 64:187-196.
    • (1993) Biophys. J. , vol.64 , pp. 187-196
    • Kawai, M.1    Wray, J.S.2    Zhao, Y.3
  • 23
    • 0029863187 scopus 로고    scopus 로고
    • Fluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor and contracting muscle
    • Ling, N., C. Shrimpton, J. Sleep, J. Kendrick-Jones, and M. Irving. 1996. Fluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor and contracting muscle. Biophys. J. 70:1836-1846.
    • (1996) Biophys. J. , vol.70 , pp. 1836-1846
    • Ling, N.1    Shrimpton, C.2    Sleep, J.3    Kendrick-Jones, J.4    Irving, M.5
  • 24
    • 0026043263 scopus 로고
    • X-ray studies of order-disorder transitions in the myosin heads of skinned rabbit psoas muscles
    • Lowy, J., D. Popp, and A. Stewart. 1991. X-ray studies of order-disorder transitions in the myosin heads of skinned rabbit psoas muscles. Biophys. J. 60:812-824.
    • (1991) Biophys. J. , vol.60 , pp. 812-824
    • Lowy, J.1    Popp, D.2    Stewart, A.3
  • 25
    • 0015974052 scopus 로고
    • The site of force generation in muscle contraction as deduced from fluorescence polarization studies
    • Nihei, T., R. A. Mendelson, and J. Botts. 1974. The site of force generation in muscle contraction as deduced from fluorescence polarization studies. Proc. Natl. Acad. Sci. USA. 71:274-277.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 274-277
    • Nihei, T.1    Mendelson, R.A.2    Botts, J.3
  • 26
    • 0020015131 scopus 로고
    • Preparation of troponin and its subunits
    • Potter, J. D. 1982. Preparation of troponin and its subunits. Methods Enzymol. 85:241-263.
    • (1982) Methods Enzymol. , vol.85 , pp. 241-263
    • Potter, J.D.1
  • 29
    • 0028962794 scopus 로고
    • Orientational dynamics of indane dione spin labeled myosin heads in relaxed and contracting skeletal muscle fibers
    • Roopnarine, O., and D. D. Thomas. 1995. Orientational dynamics of indane dione spin labeled myosin heads in relaxed and contracting skeletal muscle fibers. Biophys. J. 68:1461-1471.
    • (1995) Biophys. J. , vol.68 , pp. 1461-1471
    • Roopnarine, O.1    Thomas, D.D.2
  • 30
    • 0027050253 scopus 로고
    • Chimeric myosin regulatory light chains identify the subdomain responsible for regulatory function
    • Rowe, T., and J. Kendrick-Jones. 1992. Chimeric myosin regulatory light chains identify the subdomain responsible for regulatory function. EMBO J. 11:4715-4722.
    • (1992) EMBO J. , vol.11 , pp. 4715-4722
    • Rowe, T.1    Kendrick-Jones, J.2
  • 31
    • 0345313518 scopus 로고
    • Orientation of acetamidotetramethylrhodamine (ATR) isomers covalently bound to regulatory light chains in rabbit psoas muscle fibers
    • Sabido-David, C., J. S. Craik, B. Brandmeier, J. E. T. Corrie, D. R. Trentham, N. Ling, and M. Irving. 1994. Orientation of acetamidotetramethylrhodamine (ATR) isomers covalently bound to regulatory light chains in rabbit psoas muscle fibers. Biophys. J. 66:A234.
    • (1994) Biophys. J. , vol.66
    • Sabido-David, C.1    Craik, J.S.2    Brandmeier, B.3    Corrie, J.E.T.4    Trentham, D.R.5    Ling, N.6    Irving, M.7
  • 32
    • 0023912174 scopus 로고
    • Characterization of the myosin adenosine triphosphate (M·ATP) cross-bridge in rabbit and frog skeletal muscle fibers
    • Schoenberg, M. 1988. Characterization of the myosin adenosine triphosphate (M·ATP) cross-bridge in rabbit and frog skeletal muscle fibers. Biophys. J. 54:135-148.
    • (1988) Biophys. J. , vol.54 , pp. 135-148
    • Schoenberg, M.1
  • 33
    • 0025231857 scopus 로고
    • Temperature control and exchange of the bathing solution for skinned muscle fibers
    • Sleep, J. 1990. Temperature control and exchange of the bathing solution for skinned muscle fibers. J. Physiol. (Lond.). 423:7P.
    • (1990) J. Physiol. (Lond.) , vol.423
    • Sleep, J.1
  • 34
    • 0026513108 scopus 로고
    • Transients in orientation of a fluorescent cross-bridge probe following photolysis of caged nucleotides in skeletal muscle fibers
    • Tanner, J. W., D. D. Thomas, and Y. E. Goldman. 1992. Transients in orientation of a fluorescent cross-bridge probe following photolysis of caged nucleotides in skeletal muscle fibers. J. Mol. Biol. 223: 185-203.
    • (1992) J. Mol. Biol. , vol.223 , pp. 185-203
    • Tanner, J.W.1    Thomas, D.D.2    Goldman, Y.E.3
  • 35
    • 0016756968 scopus 로고
    • Polarization from a helix of fluorophores and its relation to that obtained from muscle
    • Tregear, R. T., and R. M. Mendelson. 1975. Polarization from a helix of fluorophores and its relation to that obtained from muscle. Biophys. J. 15:455-467.
    • (1975) Biophys. J. , vol.15 , pp. 455-467
    • Tregear, R.T.1    Mendelson, R.M.2
  • 36
    • 0027419741 scopus 로고
    • Chimeric regulatory light chains as probes of smooth muscle myosin function
    • Trybus, K. M., and T. A. Chatman. 1993. Chimeric regulatory light chains as probes of smooth muscle myosin function. J. Biol. Chem. 268: 4412-4419.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4412-4419
    • Trybus, K.M.1    Chatman, T.A.2
  • 37
    • 0023788801 scopus 로고
    • Domains, motions and regulation in the myosin head
    • Vibert, P., and C. Cohen. 1988. Domains, motions and regulation in the myosin head. J. Muscle Res. Cell Motil. 9:296-305.
    • (1988) J. Muscle Res. Cell Motil. , vol.9 , pp. 296-305
    • Vibert, P.1    Cohen, C.2
  • 38
    • 0021083489 scopus 로고
    • A comparison of order and orientation of cross-bridges in rigor and relaxed muscle fibres using fluorescence polarization
    • Wilson, M. G. A., and R. A. Mendelson. 1983. A comparison of order and orientation of cross-bridges in rigor and relaxed muscle fibres using fluorescence polarization. J. Muscle Res. Cell Motil. 4:671-693.
    • (1983) J. Muscle Res. Cell Motil. , vol.4 , pp. 671-693
    • Wilson, M.G.A.1    Mendelson, R.A.2
  • 39
    • 0001891718 scopus 로고
    • Structure of relaxed myosin filaments in relation to nucleotide state in vertebrate skeletal muscle
    • Wray, J. S. 1987. Structure of relaxed myosin filaments in relation to nucleotide state in vertebrate skeletal muscle. J. Muscle Res. Cell Motil. 8:62A.
    • (1987) J. Muscle Res. Cell Motil. , vol.8
    • Wray, J.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.