Purification of enolase and phosphoglycerate mutase from human brain and formation of a bienzymatic complex from them

Neuron-specific enolase and phosphoglycerate mutase with specific activities of 106 and 215 U/mg, respectively, have been purified from human brain. Hydrophobic chromatography for enolase and blue Sepharose affinity chromatography for phosphoglycerate mutase were used as the last steps of purificati...

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Bibliographic Details
Published in:	Biokhimiia (Moscow, Russia) Vol. 60; no. 5; p. 746
Main Authors:	Nazarian, K B, Simonian, S Z, Kazarian, B A, Perez, P, Climent, F
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-05-1995
Subjects:	Autoantibodies - metabolism Brain - enzymology Chromatography, Affinity Cross-Linking Reagents Humans Multienzyme Complexes - immunology Multienzyme Complexes - metabolism Phosphoglycerate Mutase - isolation & purification Phosphoglycerate Mutase - metabolism Phosphopyruvate Hydratase - isolation & purification Phosphopyruvate Hydratase - metabolism Succinimides
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Summary:	Neuron-specific enolase and phosphoglycerate mutase with specific activities of 106 and 215 U/mg, respectively, have been purified from human brain. Hydrophobic chromatography for enolase and blue Sepharose affinity chromatography for phosphoglycerate mutase were used as the last steps of purification. A heterobifunctional complex with fully preserved enolase and phosphoglycerate mutase activities was synthesized with the use of a bifunctional reagent, N-succinimidyl 3-(2-pyridyldithio)propionate. Autoantibodies to the conjugate will be used for identifying the bienzymatic complex in vivo.
ISSN:	0320-9725