Kb. Nazaryan et al., PURIFICATION OF HUMAN BRAIN ENOLASE AND PHOSPHOGLYCERATE MUTASE AND FORMATION OF THEIR BIENZYMATIC COMPLEX, Biochemistry, 60(5), 1995, pp. 559-564
Neuron-specific enolase and phosphoglycerate mutase with specific acti
vities of 106 and 215 units per mg, respectively, have been purified f
rom human brain. Hydrophobic chromatography on octyl-Sepharose for eno
lase and affinity chromatography on blue Sepharose for phosphoglycerat
e mutase were used as the last steps of purification. A hetero-bifunct
ional complex with fully preserved enolase and phosphoglycerate mutase
activities was synthesized using a bifunctional reagent, N-succinimid
yl-3-(2-pyridyldithio)propionate.