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Ornithine aminotransferase was purified by conventional biochemical methods from rat kidney, rat liver, and human liver. Affinity-purified antibodies raised to the rat kidney enzyme were used to produce an immunoadsorbent enabling a one-step purification of ornithine aminotransferase to be made from crude human liver extracts. The harsh chemical conditions often required to desorb immunoadsorbents were avoided by isolating antibodies with low functional affinity and employing an electrophoretic desorption method which allowed the enzyme activity to be retained. The close structural similarity between human and rat ornithine aminotransferase was demonstrated by immunodiffusion reactions. It was therefore possible to purify the enzyme from human liver using immobilized antibodies raised against rat kidney ornithine aminotransferase. Furthermore, desorption was more readily achieved due to the lower affinity for the human enzyme.
J M Leah, and
E E Billett, and
T Palmer
April 1984,
Experientia,
J M Leah, and
E E Billett, and
T Palmer
January 2000,
Blood purification,
J M Leah, and
E E Billett, and
T Palmer
January 1971,
Enzyme,
J M Leah, and
E E Billett, and
T Palmer
July 1995,
Journal of biochemistry,
J M Leah, and
E E Billett, and
T Palmer
January 1982,
The Biochemical journal,
J M Leah, and
E E Billett, and
T Palmer
December 1973,
Comparative biochemistry and physiology. B, Comparative biochemistry,
J M Leah, and
E E Billett, and
T Palmer
August 1976,
Biotechnology and bioengineering,
J M Leah, and
E E Billett, and
T Palmer
December 1972,
Comptes rendus hebdomadaires des seances de l'Academie des sciences. Serie D: Sciences naturelles,
J M Leah, and
E E Billett, and
T Palmer
January 1974,
Developments in biological standardization,
J M Leah, and
E E Billett, and
T Palmer
July 1990,
Journal of biochemistry,
