Substructure of the myosin molecule. II. The light chains of myosin.
暂无分享,去创建一个
[1] A. Weeds. Small sub-units of myosin. , 1967, The Biochemical journal.
[2] P. Butler,et al. The use of maleic anhydride for the reversible blocking of amino groups in polypeptide chains. , 1969, The Biochemical journal.
[3] F. Morita. Interaction of heavy meromyosin with substrate. I. Difference in ultraviolet absorption spectrum between heavy meromyosin and its Michaelis-Menten complex. , 1967, The Journal of biological chemistry.
[4] F. Pepe. SOME ASPECTS OF THE STRUCTURAL ORGANIZATION OF THE MYOFIBRIL AS REVEALED BY ANTIBODY-STAINING METHODS , 1966, The Journal of cell biology.
[5] J. Gergely,et al. The conformation of myosin during the steady state of ATP hydrolysis: studies with myosin spin labeled at the S 1 thiol groups. , 1971, Biochemical and biophysical research communications.
[6] C. Suelter,et al. A simple chromatographic procedure for the preparation of rabbit-muscle myosin A free from AMP deaminase. , 1967, Biochimica et biophysica acta.
[7] A. Martonosi,et al. Kinetics and substrate binding of myosin adenosine triphosphatase. , 1968, The Journal of biological chemistry.
[8] R. J. Clark,et al. The Conformation of Native and Denatured Tropomyosin B , 1965 .
[9] H. Huxley. Structural difference between resting and rigor muscle; evidence from intensity changes in the lowangle equatorial x-ray diagram. , 1968, Journal of molecular biology.
[10] M. Morales,et al. Independent and cooperative reactions of myosin heads with F-actin in the presence of adenosine triphosphate. , 1971, Biochemistry.
[11] J. E. Godfrey,et al. Self-association in the myosin system at high ionic strength. II. Evidence for the presence of a monomer--dimer equilibrium. , 1970, Biochemistry.
[12] T. Tsao. Fragmentation of the myosin molecule. , 1953, Biochimica et biophysica acta.
[13] A. Holtzer,et al. The Molecular Weight, Size and Shape of the Myosin Molecule , 1956 .
[14] A. Rizzino,et al. Actin-heavy meromyosin biding. Determination of binding stoichiometry from adenosine triphosphatase kinetic measurements. , 1970, Biochemistry.
[15] D. Kominz. Molecular changes in myosin caused by methylmercuric hydroxide. , 1961, Biochimica et biophysica acta.
[16] George A. Bray,et al. A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counter , 1960 .
[17] K. Takahashi,et al. WATER-SOLUBLE SUBFRACTION IN MYOSIN A PREPARATION. , 1963, Journal of biochemistry.
[18] S. Perry,et al. The chromatography of the meromyosins on diethylaminoethylcellulose. , 1961, The Biochemical journal.
[19] C. Dent. The amino-aciduria in Fanconi syndrome. A study making extensive use of techniques based on paper partition chromatography. , 1947, The Biochemical journal.
[20] W. Mommaerts,et al. Studies on myosin. II. Some molecular-kinetic data. , 1954, The Journal of biological chemistry.
[21] A. Stracher. Evidence for the involvement of light chains in the biological functioning of myosin. , 1969, Biochemical and biophysical research communications.
[22] D. Caspar,et al. Tropomyosin: crystal structure, polymorphism and molecular interactions. , 1969, Journal of molecular biology.
[23] S. Lowey. COMPARATIVE STUDY OF THE ALPHA-HELICAL MUSCLE PROTEINS. TYROSYL TITRATION AND EFFECT OF PH ON CONFORMATION. , 1965, Journal of Biological Chemistry.
[24] S. Waley,et al. The action of trypsin on polylysine. , 1953, The Biochemical journal.
[25] M. Perutz,et al. Structure of Hæmoglobin: A Three-Dimensional Fourier Synthesis at 5.5-Å. Resolution, Obtained by X-Ray Analysis , 1960, Nature.
[26] R. V. Rice. Conformation of individual macromolecular particles from myosin solutions , 1961 .
[27] A. Szent-Györgyi. Meromyosins, the subunits of myosin , 1953 .
[28] J. Maizel,et al. Molecular weight estimation of polypeptides by SDS-polyacrylamide gel electrophoresis: further data concerning resolving power and general considerations. , 1969, Analytical biochemistry.
[29] L. Gershman,et al. Subunit structure of myosin. 3. A proposed model for rabbit skeletal myosin. , 1969, The Journal of biological chemistry.
[30] J. R. Brown,et al. Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A. , 1966, The Biochemical journal.
[31] P. Dreizen,et al. Relationship of structure to function in myosin. I. Subunit dissociation in concentrated salt solutions. , 1970, Biochemistry.
[32] E. G. Richards,et al. Chromatography of myosin on diethylaminoethyl-Sephadex A-50. , 1967, Biochemistry.
[33] S. Himmelfarb,et al. Studies on the subunit structure of myosin. , 1970, The Journal of biological chemistry.
[34] A. Holtzer,et al. The substructure of the myosin molecule. Production and properties of the alkali subunits. , 1968, Biochemistry.
[35] S. Perry,et al. The degradation of heavy meromyosin by trypsin. , 1962, The Biochemical journal.
[36] D. Segal,et al. Composition and mass of peptides released during tryptic and chymotryptic hydrolysis of myosin. , 1967, The Journal of biological chemistry.
[37] H. Huxley,et al. ELECTRON MICROSCOPE STUDIES ON THE STRUCTURE OF NATURAL AND SYNTHETIC PROTEIN FILAMENTS FROM STRIATED MUSCLE. , 1963, Journal of molecular biology.
[38] C. Cohen,et al. Studies on the structure of myosin. , 1962, Journal of molecular biology.
[39] K. Weber,et al. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. , 1969, The Journal of biological chemistry.
[40] F. Irreverre. A modified Sakaguchi spray. , 1965, Biochimica et biophysica acta.
[41] E. Taylor,et al. Mechanism of adenosine triphosphate hydrolysis by actomyosin. , 1971, Biochemistry.
[42] S. Lowey,et al. Equilibrium binding of adenosine diphosphate to myosin. , 1969, Biochemistry.
[43] K. Bárány,et al. Polydispersity of succinylated myosin. , 1966, Archives of biochemistry and biophysics.
[44] A. Szent-Gyorgyi,et al. Trypsin digestion of muscle proteins. I. Ultracentrifugal analysis of the process. , 1953, The Journal of biological chemistry.
[45] H. Mueller. Characterization of the molecular region containing the active sites of myosin. , 1965, The Journal of biological chemistry.
[46] E. Eisenberg,et al. The adenosine triphosphatase activity of acto-heavy meromyosin. A kinetic analysis of actin activation. , 1968, Biochemistry.
[47] C. Cohen,et al. Proteolytic degradation of myosin and the meromyosins by a water-insoluble polyanionic derivative of trypsin: properties of a helical subunit isolated from heavy meromyosin. , 1967, Journal of molecular biology.
[48] E. Mihályi,et al. Studies on the tryptic digestion of myosin , 1959 .
[49] G. Scatchard,et al. THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS , 1949 .
[50] S. Perry. The chromatography of L-myosin on diethylaminoethylcellulose. , 1960, The Biochemical journal.
[51] P. Trotta,et al. Myosin Subunits and their interactions , 1967 .
[52] J. Botts. Typical behaviour of some simple models of enzyme action , 1958 .
[53] D. A. Yphantis. EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS. , 1964, Biochemistry.
[54] A. Oplatka,et al. On the formation and stability of the enzymically active complexes of heavy meromyosin with actin. , 1969, Journal of molecular biology.
[55] D. Givol,et al. A two-stage cleavage of rabbit gamma-globulin by a water-insoluble papain preparation followed by cysteine. , 1961, The Journal of biological chemistry.
[56] S. Perry,et al. An electrophoretic study of the low-molecular-weight components of myosin. , 1970, The Biochemical journal.
[57] C. Hirs. The oxidation of ribonuclease with performic acid. , 1956, The Journal of biological chemistry.
[58] L. Szilágyi,et al. Studies on proteins and protein complexes of muscle by means of proteolysis. V. Fragmentation of light meromyosin by trypsin. , 1968, Journal of molecular biology.
[59] R. G. Harrison,et al. Assembly of myosin. , 1971, Journal of molecular biology.
[60] E. Eisenberg,et al. Subfragment 1 of myosin: adenosine triphophatase activation by actin. , 1968, Biochemistry.
[61] G. Ellman,et al. Tissue sulfhydryl groups. , 1959, Archives of biochemistry and biophysics.
[62] C. Kay,et al. The Papain Digestion of Skeletal Myosin A , 1965 .
[63] P. Gordon,et al. Potentiation by Adrenaline of a Proteolytic Activity Associated with Purified Myosin , 1963, Science.
[64] J. Gergely. Studies on myosin-adenosinetriphosphatase. , 1953, The Journal of biological chemistry.
[65] J. Kirkwood,et al. The Intrinsic Viscosity, Translational and Rotatory Diffusion Constants of Rod‐Like Macromolecules in Solution , 1950 .
[66] K. Holmes,et al. Induced Changes in Orientation of the Cross-Bridges of Glycerinated Insect Flight Muscle , 1965, Nature.
[67] I. Smith,et al. ‘Multiple Dipping’ Procedures in Paper Chromatography: a Specific Test for Hydroxy-proline , 1953, Nature.
[68] S. Lowey,et al. Light Chains from Fast and Slow Muscle Myosins , 1971, Nature.
[69] A. Weeds. Light Chains of Myosin , 1969, Nature.
[70] C. Hagyard,et al. Small subunits in myosin. , 1967, Archives of biochemistry and biophysics.
[71] R. E. OFFORD,et al. Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide Groups , 1966, Nature.
[72] B. Matthews,et al. Three-dimensional Structure of Tosyl-α-chymotrypsin , 1967, Nature.
[73] J. Spudich,et al. 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. , 1971, The Journal of biological chemistry.
[74] H. Mueller. MOLECULAR WEIGHT OF MYOSIN AND MEROMYOSINS BY ARCHIBALD EXPERIMENTS PERFORMED WITH INCREASING SPEED OF ROTATIONS. , 1964, The Journal of biological chemistry.
[75] M. Young,et al. Studies on the isolation and molecular properties of homogeneous globular actin. Evidence for a single polypeptide chain structure. , 1967, The Journal of biological chemistry.
[76] C. Hagyard,et al. Variations in the small subunits of different myosins. , 1967, Archives of biochemistry and biophysics.
[77] T. Shimizu,et al. Interaction of heavy meromyosin with substrate. 3. Difference spectrum of ultraviolet absorption in subfragment I induced by ATP or ADP. , 1969, Biochimica et biophysica acta.
[78] S. Asakura. The interaction between G-actin and ATP. , 1961, Archives of biochemistry and biophysics.
[79] M. Bárány,et al. The binding of adenosine triphosphate to myosin. , 1968, Biochemistry.
[80] K. Holmes,et al. X-ray diffraction evidence for α-helical coiled-coils in native muscle , 1963 .
[81] W. Barouch,et al. Effect of temperature on actin activation of heavy meromyosin ATPase. , 1971, Biochimica et biophysica acta.
[82] F. Pepe. The myosin filament. I. Structural organization from antibody staining observed in electron microscopy. , 1967, Journal of molecular biology.
[83] C. H. Fiske,et al. THE COLORIMETRIC DETERMINATION OF PHOSPHORUS , 1925 .
[84] J. Eccleston,et al. Elementary processes of the magnesium ion-dependent adenosine triphosphatase activity of heavy meromyosin. A transient kinetic approach to the study of kinases and adenosine triphosphatases and a colorimetric inorganic phosphate assay in situ. , 1972, The Biochemical journal.
[85] F. D. Carlson,et al. An electron microscopic investigation of myosin and some of its aggregates. , 1963, Journal of molecular biology.
[86] M. Bárány,et al. Studies on the low molecular weight protein components in rabbit skeletal myosin. , 1968, Archives of biochemistry and biophysics.
[87] A. Martonosi,et al. The regulation of the rate of ATP hydrolysis by H-meromyosin. , 1972, Archives of biochemistry and biophysics.
[88] R. Cooke,et al. Interaction of globular actin with myosin subfragments. , 1971, Journal of molecular biology.
[89] A. Holtzer,et al. ON THE STRUCTURE OF THE PARAMYOSIN MOLECULE. , 1963, Journal of molecular biology.
[90] R. Strohman,et al. Myosin structure as revealed by simultaneous electrophoresis of heavy and light subunits. , 1970, Biochemistry.
[91] A. Szent-Györgyi,et al. Fluorescence studies on heavy meromyosin-substrate interaction. , 1972, Biochemistry.
[92] R. V. Rice. An electron microscopical examination of configurations of ribonucleic acid and other polyelectrolytes. , 1961, Biochimica et biophysica acta.
[93] J. Gergely,et al. Interaction of actomyosin with adenosine triphosphate at low ionic strength. I. Dis-sociation of actomyosin during the clear phase. , 1962, The Journal of biological chemistry.
[94] B. Hartley,et al. Selective purification of the thiol peptides of myosin. , 1968, The Biochemical journal.
[95] E. Eisenberg,et al. Actin activation of heavy meromyosin adenosine triphosphatase. Dependence on adenosine triphosphate and actin concentrations. , 1970, The Journal of biological chemistry.
[96] S. Himmelfarb,et al. ON THE STRUCTURAL ASSEMBLY OF THE POLYPEPTIDE CHAINS OF HEAVY MEROMYOSIN. , 1965, The Journal of biological chemistry.
[97] H E Huxley,et al. The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. , 1967, Journal of molecular biology.
[98] S. Lowey,et al. Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation. , 1969, Journal of molecular biology.
[99] C. Hagyard,et al. The myosin of rabbit red muscles. , 1968, Archives of biochemistry and biophysics.
[100] C. Cohen,et al. Light meromyosin fraction I: A helical molecule from myosin , 1960 .
[101] S. Perry,et al. The biological activity of subfragment 1 prepared from heavy meromyosin. , 1966, The Biochemical journal.
[102] M. Young. On the interaction of adenosine diphosphate with myosin and its enzymically active fragments. Evidence for three identical catalytic sites per myosin molecule. , 1967, The Journal of biological chemistry.
[103] L. Cohen,et al. Rheological and spray properties of dilute polymer solutions , 1961 .
[104] W. Carroll,et al. A subunit of myosin , 1959 .
[105] E. Taylor,et al. Transient state phosphate production in the hydrolysis of nucleoside triphosphates by myosin. , 1970, Biochemistry.
[106] P. Cooke,et al. In vitro synthesis of light and heavy polypeptide chains of myosin. , 1970, Biochemical and biophysical research communications.
[107] P. Dreizen,et al. Relationship of structure to function in myosin. II. Salt denaturation and recombination experiments. , 1970, Biochemistry.