Application of high performance liquid chromatography to the preparation of encephalitogenic myelin basic protein

Two preparations of myelin basic protein (MBP) were derived from an acid excretion of chloroform-methanol defatted bovine spinal cord. The first was purified by ion-exchange chromatography using guanidine-HCl; the second, by high performance liquid chromatography (HPLC) using a triethylamine eluant. Both methods of preparation yield MBP which is identical on acid-urea polyacrylamide gel electrophoresis and which has identical encephalitogenic potency. Because of the greater time-efficiency of the HPLC system with no deleterious side effects due to buffer contamination, this latter method can be recommended for MBP purification.