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PHYSICAL PROPERTIES OF THE BOVINE ENCEPHALITOGENIC PROTEIN; MOLECULAR WEIGHT AND CONFORMATION 1
Author(s) -
Chao L.P.,
Einstein Elizabeth Roboz
Publication year - 1970
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1970.tb03360.x
Subject(s) - guanidine , chemistry , sedimentation coefficient , sedimentation equilibrium , intrinsic viscosity , viscosity , optical rotatory dispersion , partial specific volume , sephadex , hydrochloride , sedimentation , size exclusion chromatography , dispersion (optics) , chromatography , ultracentrifuge , crystallography , thermodynamics , biochemistry , organic chemistry , circular dichroism , paleontology , physics , sediment , optics , enzyme , polymer , biology
— The highly basic encephalitogenic protein isolated from bovine spinal cord was studied by various physicochemical methods:1 The molecular weight was determined by sedimentation equilibrium, by calculation from the data on sedimentation coefficients and intrinsic viscosities, by measurement of intrinsic viscosity in the presence of concentrated guanidine hydrochloride (according to the method of T anford , K awahara and L apanie , 1967), and by exclusion chromatography on Sephadex G‐100 columns. All values obtained were in good agreement and indicated a molecular weight of approximately 18,000–20,000.2 Studies of sedimentation velocities in the presence and absence of 6 m ‐guanidine‐HCl indicated that there was a significant difference in the values of sedimentation coefficients.3 The same conditions were applied to the measurements of viscosity; the difference was small but significant. These findings and the magnitude of the intrinsic viscosity suggested that this protein was in a disordered configuration. From these data, it is concluded that the protein was apparently monodispersed, in the presence or absence of the denaturing agent. This protein behaved like a polyelectrolyte in neutral aqueous solution.4 The measurements of optical rotatory dispersion also confirmed that this protein existed in a disordered configuration.