Purification of liver aldehyde dehydrogenase by p-hydroxyacetophenone-Sepharose affinity matrix and the coelution of chloramphenicol acetyl transferase from the same matrix with recombinantly expressed aldehyde dehydrogenase

Author:

Ghenbot Ghiorghis,Weiner Henry

Publisher

Elsevier BV

Subject

Biotechnology

Reference42 articles.

1. Aldehyde dehydrogenase mechanism of action and possible physiological roles;Weiner,1979

2. Horse liver aldehyde dehydrogenase. I. Purification and characterization;Feldman;J. Biol. Chem,1972

3. Two aldehyde dehydrogenases from human liver. Isolation via affinity chromatography and characterization of the isozymes;Greenfield;Biochem. Biophys. Acts,1977

4. Identification of the cysteine residue in the active site of horse liver mitochondrial aldehyde dehydrogenase;Tu;J. Biol. Chem,1988

5. The use of pH-gradient ion-exchange chromatography to separate sheep liver cytoplasmic aldehyde dehydrogenase from mitochondrial enzyme contamination, and observations on the interactions between the pure cytoplasmic enzyme and disulfiram;Dickinson;Biochem. J,1981

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