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Volumn 119, Issue 1, 1996, Pages 151-156

Maleimidobenzoyl actin: Its biochemical properties and in vitro motility

Author keywords

Actin actin interface; Actin myosin interaction; Ca2+ regulation; Hetero bifunctional reagent; In vitro motility assay

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE (MAGNESIUM); CALCIUM ION; MALEIMIDE DERIVATIVE; MYOSIN; MYOSIN HEAVY CHAIN; MYOSIN SUBFRAGMENT 1; PHALLOIDIN; POTASSIUM CHLORIDE; SODIUM CHLORIDE; TROPOMYOSIN; TROPONIN;

EID: 0030049459     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021200     Document Type: Article
Times cited : (7)

References (32)
  • 1
    • 0024406414 scopus 로고
    • Coupling of nonpolymerizable monomeric actin to the F-actin binding region of the myosin head
    • Bettache, N., Bertrand, R., and Kassab, R. (1989) Coupling of nonpolymerizable monomeric actin to the F-actin binding region of the myosin head. Proc. Natl. Acad. Sci. USA 86, 6028-6032
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6028-6032
    • Bettache, N.1    Bertrand, R.2    Kassab, R.3
  • 2
    • 0025102695 scopus 로고
    • Maleimidobenzoyl-G-actin: Structural properties and interaction with skeletal myosin subfragment-1
    • Bettache, N., Bertrand, R., and Kassab, R. (1990) Maleimidobenzoyl-G-actin: Structural properties and interaction with skeletal myosin subfragment-1. Biochemistry 29, 9085-9091
    • (1990) Biochemistry , vol.29 , pp. 9085-9091
    • Bettache, N.1    Bertrand, R.2    Kassab, R.3
  • 3
    • 0025966670 scopus 로고
    • Interaction of nonpolymerizable actins with myosin
    • Arata, T. (1991) Interaction of nonpolymerizable actins with myosin. J. Biochem. 109, 335-340
    • (1991) J. Biochem. , vol.109 , pp. 335-340
    • Arata, T.1
  • 4
    • 0025816962 scopus 로고
    • Interaction of maleimidobenzoyl actin with myosin subfragment 1 and tropomyosin troponin
    • Miki, M. and Hozumi, T. (1991) Interaction of maleimidobenzoyl actin with myosin subfragment 1 and tropomyosin troponin. Biochemistry 30, 5625-5630
    • (1991) Biochemistry , vol.30 , pp. 5625-5630
    • Miki, M.1    Hozumi, T.2
  • 6
    • 0021748193 scopus 로고
    • Modification of actin with fluorescein isothiocyanate
    • Burtnick, L.D. (1984) Modification of actin with fluorescein isothiocyanate. Biochim. Biophys. Acta 791, 57-62
    • (1984) Biochim. Biophys. Acta , vol.791 , pp. 57-62
    • Burtnick, L.D.1
  • 7
    • 0023090644 scopus 로고
    • The recovery of the polymerizability of Lys-61-labelled actin by the addition of phalloidin. Fluorescence polarization and resonance-energy-transfer measurements
    • Miki, M. (1987) The recovery of the polymerizability of Lys-61-labelled actin by the addition of phalloidin. Fluorescence polarization and resonance-energy-transfer measurements. Eur. J. Biochem. 164, 229-235
    • (1987) Eur. J. Biochem. , vol.164 , pp. 229-235
    • Miki, M.1
  • 8
    • 0025075839 scopus 로고
    • Atomic model of the actin filament
    • Holmes, K.C., Popp, D., Gebhard, W., and Kabsch, W. (1990) Atomic model of the actin filament. Nature 347, 44-49
    • (1990) Nature , vol.347 , pp. 44-49
    • Holmes, K.C.1    Popp, D.2    Gebhard, W.3    Kabsch, W.4
  • 9
    • 0013877728 scopus 로고
    • On the molecular weight of myosin. II
    • Tonomura, Y., Appel, P., and Morales, M.F. (1966) On the molecular weight of myosin. II. Biochemistry 5, 515-521
    • (1966) Biochemistry , vol.5 , pp. 515-521
    • Tonomura, Y.1    Appel, P.2    Morales, M.F.3
  • 10
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J.A. and Watt, S. (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246, 4866-4871
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 11
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility
    • Weeds, A.G. and Pope, B. (1977) Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111, 129-157
    • (1977) J. Mol. Biol. , vol.111 , pp. 129-157
    • Weeds, A.G.1    Pope, B.2
  • 12
    • 0025339318 scopus 로고
    • In vitro motility of skeletal muscle myosin and its proteolytic fragments
    • Takiguchi, K., Hayashi, H., Kurimoto, E., and Higashi-Fujime, S. (1990) In vitro motility of skeletal muscle myosin and its proteolytic fragments. J. Biochem. 107, 671-679
    • (1990) J. Biochem. , vol.107 , pp. 671-679
    • Takiguchi, K.1    Hayashi, H.2    Kurimoto, E.3    Higashi-Fujime, S.4
  • 13
    • 0014975959 scopus 로고
    • Studies on enzymatically active subfragments of myosin-adenosine triphosphatase. I. Preparation using chymotrypsin
    • Onodera, M. and Yagi, K. (1971) Studies on enzymatically active subfragments of myosin-adenosine triphosphatase. I. Preparation using chymotrypsin. J. Biochem. 69, 145-153
    • (1971) J. Biochem. , vol.69 , pp. 145-153
    • Onodera, M.1    Yagi, K.2
  • 14
    • 0015840125 scopus 로고
    • The subunits and biological activity of polymorphic forms of tropomyosin
    • Cummins, P. and Perry, S.V. (1973) The subunits and biological activity of polymorphic forms of tropomyosin. Biochem. J. 133, 765-777
    • (1973) Biochem. J. , vol.133 , pp. 765-777
    • Cummins, P.1    Perry, S.V.2
  • 15
    • 0015527223 scopus 로고
    • Effect of calcium ions on the flexibility of reconstituted thin filaments of muscle studied by quasielastic scattering of laser light
    • Ishiwata, S. and Fujime, S. (1972) Effect of calcium ions on the flexibility of reconstituted thin filaments of muscle studied by quasielastic scattering of laser light. J. Mol. Biol. 68, 511-522
    • (1972) J. Mol. Biol. , vol.68 , pp. 511-522
    • Ishiwata, S.1    Fujime, S.2
  • 16
    • 0015526770 scopus 로고
    • Intrinsic fluorescence of actin
    • Lehrer, S.S. and Kerwar, G. (1972) Intrinsic fluorescence of actin. Biochemistry 11, 1211-1217
    • (1972) Biochemistry , vol.11 , pp. 1211-1217
    • Lehrer, S.S.1    Kerwar, G.2
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, N.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72, 248-254
    • (1976) Anal Biochem. , vol.72 , pp. 248-254
    • Bradford, N.M.1
  • 18
  • 19
    • 0021261156 scopus 로고
    • Direct observation of motion of single F-actin filaments in the presence of myosin
    • Yanagida, T., Nakase, M., Nishiyama, K., and Oosawa, F. (1984) Direct observation of motion of single F-actin filaments in the presence of myosin. Nature 307, 58-60
    • (1984) Nature , vol.307 , pp. 58-60
    • Yanagida, T.1    Nakase, M.2    Nishiyama, K.3    Oosawa, F.4
  • 20
    • 0023919181 scopus 로고
    • Force measurements by micromanipulation of a single actin filament by glass needles
    • Kishino, A. and Yanagida, T. (1988) Force measurements by micromanipulation of a single actin filament by glass needles. Nature 334, 74-76
    • (1988) Nature , vol.334 , pp. 74-76
    • Kishino, A.1    Yanagida, T.2
  • 21
    • 0025817087 scopus 로고
    • Reconstitution of active movement in vitro based on the actin myosin interaction
    • Higashi-Fujime, S. (1991) Reconstitution of active movement in vitro based on the actin myosin interaction. Int. Rev. Cytol. 125, 95-138
    • (1991) Int. Rev. Cytol. , vol.125 , pp. 95-138
    • Higashi-Fujime, S.1
  • 22
    • 0020632188 scopus 로고
    • Structure and function of myosin subfragment 1 as studied by tryptic digestion
    • Hozumi,T. (1983) Structure and function of myosin subfragment 1 as studied by tryptic digestion. Biochemistry 22, 799-804
    • (1983) Biochemistry , vol.22 , pp. 799-804
    • Hozumi, T.1
  • 23
    • 0021348581 scopus 로고
    • Actin-actin and actin deoxyribonuclease I contact sites in the actin sequence
    • Sutoh, K. (1984) Actin-actin and actin deoxyribonuclease I contact sites in the actin sequence. Biochemistry 23, 1942-1946
    • (1984) Biochemistry , vol.23 , pp. 1942-1946
    • Sutoh, K.1
  • 24
    • 0019877189 scopus 로고
    • Isolation and characterization of covalently cross-linked actin dimer
    • Mockrin, S.C. and Korn, E.D. (1981) Isolation and characterization of covalently cross-linked actin dimer. J. Biol. Chem. 256, 8228-8233
    • (1981) J. Biol. Chem. , vol.256 , pp. 8228-8233
    • Mockrin, S.C.1    Korn, E.D.2
  • 26
    • 0025685506 scopus 로고
    • Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility
    • Prochniewicz, E. and Yanagida, T. (1990) Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility. J. Mol. Biol. 216, 761 772
    • (1990) J. Mol. Biol. , vol.216 , pp. 761772
    • Prochniewicz, E.1    Yanagida, T.2
  • 27
    • 0019890802 scopus 로고
    • Change of reactivity of lysine residues upon actin polymerization
    • Lu, R.C. and Szilagyi, L. (1981) Change of reactivity of lysine residues upon actin polymerization. Biochemistry 20, 5914-5919
    • (1981) Biochemistry , vol.20 , pp. 5914-5919
    • Lu, R.C.1    Szilagyi, L.2
  • 28
    • 0024422304 scopus 로고
    • Interaction of Lys-61 labeled actin with myosin subfragment-1 and the regulatory proteins
    • Miki, M. (1989) Interaction of Lys-61 labeled actin with myosin subfragment-1 and the regulatory proteins. J. Biochem. 106, 651 655
    • (1989) J. Biochem. , vol.106 , pp. 651-655
    • Miki, M.1
  • 29
    • 0026540802 scopus 로고
    • Covalent modification of G-actin by pyridoxal 5′-phosphate: Polymerization properties and interaction with DNase I and myosin subfragment 1
    • Combeau, C. and Carlier, M.-F. (1992) Covalent modification of G-actin by pyridoxal 5′-phosphate: Polymerization properties and interaction with DNase I and myosin subfragment 1. Biochemistry 31, 300-309
    • (1992) Biochemistry , vol.31 , pp. 300-309
    • Combeau, C.1    Carlier, M.-F.2
  • 30
  • 31
    • 0020479817 scopus 로고
    • Changes in actin lysine reactivities during polymerization detected using a competitive labeling method
    • Hitchcock-De Gregori, S.E., Mandala, S., and Sachs, G.A. (1982) Changes in actin lysine reactivities during polymerization detected using a competitive labeling method. J. Biol. Chem. 257, 12573 12580
    • (1982) J. Biol. Chem. , vol.257 , pp. 12573-12580
    • Hitchcock-De Gregori, S.E.1    Mandala, S.2    Sachs, G.A.3
  • 32
    • 0026806428 scopus 로고
    • Actin actin contact: Inhibition of actin-polymerization by subdomain 4 peptide fragments
    • Hori, K. and Monta, F. (1992) Actin actin contact: Inhibition of actin-polymerization by subdomain 4 peptide fragments. J. Biochem. 112, 401-408
    • (1992) J. Biochem. , vol.112 , pp. 401-408
    • Hori, K.1    Monta, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.