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Biochemical purification of monkey and human LDH isoenzyme 5 suitable as immunization antigen
The Italian Journal of Biochemistry
|January 1, 1985
Abstract:
A method consisting in an ion-exchange chromatography on DEAE-Sephadex A50 and an affinity chromatography on Oxamate-hexyl-Sepharose for the purification of monkey and human LDH isoenzyme 5 is presented. Analytical isoelectric focusing reveals minor variants in the monkey LDH isoenzyme 5. This material has been used to produce an antiserum from rabbits which recognizes all the human LDH isoenzymes containing the M subunit, without cross-reacting with LDH1.