Conformation of β-casein B

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Abstract

Molecular weight and viscosity studies of β-casein B in 0.14 m NaCl, 0.02 m EDTA, pH 7, 2.5 °, and in 6.0 m Guanidine HCL, pH 7, 25 °, have led to the conclusion that the protein has a random coil conformation in both of these solvents.

References (23)

  • R.A. Sullivan et al.

    Arch. Biochem. Biophys

    (1955)
  • T.A.J. Payens et al.

    Biochim. Biophys. Acta

    (1963)
  • R.F. Peterson et al.

    Biochem. Biophys. Res. Commun

    (1966)
  • M.P. Thompson

    J. Dairy Sci

    (1966)
  • E.B. Kalan et al.

    J. Dairy Sci

    (1965)
  • C. Ho et al.

    J. Biol. Chem

    (1967)
  • G.C. Kresheck

    Acta Chem. Scand

    (1965)
  • T.T. Herskovits

    Biochemistry

    (1966)
  • R. Aschaffenburg

    J. Dairy Res

    (1963)
  • D.G. Schmidt et al.

    Neth. Milk Dairy J

    (1964)
  • S.N. Timasheff et al.

    J. Am. Chem. Soc

    (1961)
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    Eastern Utilization Research and Development Division, Agricultural Research Service, U.S. Department of Agriculture.

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