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Affinity Chromatography. Biospecific Sorption–The First by O. Hoffmann-Ostenhof

By O. Hoffmann-Ostenhof

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Indeed as F i g . 5 s h o w s , IMP d e h y d r o g e n a s e w a s eluted in a v e r y broad band f r o m I M P - S e p h a r o s e and required a p u l s e of 10 mM A M P to effect quantitative r e l e a s e . F u r t h e r m o r e , incorporation of 10 mM IMP in the equilibration buffer r e s u l t s in the appearance of the e n z y m e in a l a r g e number of fractions c o m m e n c i n g at, and with highest activity in, the void v o l u m e . Quantitative elution could be expedited by pulsing with 10 mM A M P as found p r e v i o u s l y .

2 (15) k. 1 (16) 5. 2 (11) 6. 1 (12) 7. 02 (13) 8. 05 (17) 9. 0. 1. Glutamate dehydrogenase NADP + 2«-AMP TRIAZINE-LINKED DYES AS GROUP-SPECIFIC LIGANDS We have examined alternative adsorbents for the selective purification of dehydrogenases in an attempt to overcome the above problem of capacity associated with nucleotides as ligands. Cibacron Blue F3G~A has been widely used for the purification of a number of different proteins, including dehydrogenases (20). Another triazine-linked dye Procion Red HE"3B has recently been used by Baird et^ al.

Dean and David H. Watson The relationship between the K* for NADP+'dependent dehydrogenases and the capacity is not apparent from free solution studies where the Ki's observed have been 1~2 orders of magnitude lower. This discrepancy could be explained on the basis of ligand crowding (for capacity values above the optimum ligand concentration)· Diffusional limitations within the porous gel structure must also be considered to contribute to the above discrepancy. The latter may be partly removed by eliminating the porous nature of the gel.

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