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STRUCTURAL AND IMMUNOLOGICAL PROPERTIES OF NEURON SPECIFIC PROTEIN (NSP) FROM RAT, CAT AND HUMAN BRAIN: COMPARISON TO BOVINE 14‐3‐2

Abstract— Neuron specific protein (NSP) has been isolated from cat (NSP‐C) and human (NSP‐H) brain utilizing the purification procedure described for rat brain 14‐3‐2 (Marangoset al., 1975a,b,c), a protein which is now designated NSP‐R. The protein as isolated from cat and human brain has a molecular weight of approx 80,000 as determined by sedimentation equilibrium. Sedimentation studies done in the presence of 6mg‐HCl and 0.2%β mercaptoethanol yields a protomer M.W. of approx 40,000 for both preparations establishing the dimeric nature of each. The subunits appear identical in each case since one band is observed upon electrophoresis of either preparation in the presence of 8 M‐urea. NSP‐C and NSP‐H have identical isoelectric points of 4.7 making them slightly more acidic than NSP‐R (pi = 5.0).