Further results on lipase-colipase interactions studied by affinity chromatography.
Affinity chromatography of lipase on a colipase-coupled gel was studied in the present paper. The elution volume of the associable lipase increased when the loaded amount decreased. A KD value of 1.9 X 10(-6) M at pH 6.2 was thus deduced. A minimum value of 1.5 X 10(-6) M was obtained at pH 5.1-5.3. Mixed micelles associated with coupled colipase, but no modifications of lipase-colipase interactions took place when mixed micelles were added to the elution buffer. DMMA-modified coupled colipase failed to interact with lipase, owing to the specific orientation of the modified cofactor in the gel.
D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002845:Chromatography; D002846:Chromatography, Affinity; D003089:Colipases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000378:metabolism*; D008299:Maleic Anhydrides / Q000494:pharmacology; D008823:Micelles; D011506:Proteins / Q000378:metabolism*; D013552:Swine
D003089:Colipases; D008299:Maleic Anhydrides; D008823:Micelles; D011506:Proteins; C007474:2,3-dimethylmaleic anhydride; D008049:Lipase