[Physicochemical properties of neurospecific basic protein (SCP) of the spinal cord].

Basic protein (SCP) known as antiencephalytogenic was isolated from the bull spinal cord and spinal roots. The protein is purified to a molecular homogeneous state, some of its physicochemical properties are studied. Molecular homogeneity of the protein is established by the method of disk electrophoresis in 15% polyacrylamide gel with sodium dodecyl sulphate present and by analytic ultracentrifugation. During electrophoresis in 15% polyacrylamide gel at pH 4.0 the protein movement occurs only in one zone, and at pH 7.0 three closely located zones are formed. The protein molecular weight determined by different methods is about 13500. The protein amino acid composition is determined and it is shown that 9.6 mole of amide nitrogen falls on 1 mole of the protein. The presence of the tertiary structure in the protein is supposed.