Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.6.1.1 (aspartate aminotransferase)
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Tyrosine phenol-lyase from Erwinia herbicola was purified from a cell-free extract in a single step on Cibacron Blue F3GA-agarose. The protein was purified as the apoenzyme and was unstable after affinity chromatography. Alanine aminotransferase and aspartate aminotransferase from porcine heart also bound to Cibacron Blue F3GA-agarose. These enzymes were partially purified as holoenzymes from a crude porcine heart extract by elution with NADH and KCl. Alanine aminotransferase was purified 19 fold by this procedure.
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PMID:Affinity chromatography of some pyridoxal phosphate-requiring enzymes on Cibacron Blue F3GA-agarose. 725 63

Three biomimetic dye ligands bearing as a triazine-linked terminal moiety a carboxylated structure, which mimics substrates and inhibitors of L-lactate dehydrogenase (LDH), were immobilized on cross-linked agarose Ultrogel A6R. These biomimetic dyes are purpose-designed analogues of commercial monochlorotriazine Cibacron Blue 3GA (CB3GA) and parent dichlorotriazine Vilmafix Blue A-R (VBAR). The corresponding biomimetic adsorbents, along with non-biomimetic adsorbents bearing CB3GA and VBAR, were evaluated for their ability to purify LDH from bovine heart crude extract. When compared with non-biomimetic adsorbents, all biomimetic adsorbents exhibited a higher purifying ability. Further, one immobilized biomimetic dye, bearing mercaptopyruvic acid as biomimetic moiety, displayed the highest purifying ability. The concentration of immobilized dye affected both the capacity and the purifying ability of the affinity column, exhibiting an optimum value 2.2 mumol dye/g moist gel. This affinity adsorbent was exploited for the purification of LDH from bovine heart in a two-step procedure. The procedure consisted in a biomimetic dye affinity chromatography step (NAD+/sulphite elution, 25-fold purification, 64% step yield), followed by DEAE-agarose ion-exchange chromatography (1.4-fold purification, 78% step yield). The purified enzyme exhibited a specific activity of ca. 480 u/mg at 25 degrees C (content of impurities: pyruvate kinase and glutamic-oxaloacetic transaminase were not detected; malate dehydrogenase, 0.01%), compared with ca. 250 u/mg of commercial bovine heart LDH (malate dehydrogenase, 0.05%) suitable for analytical purposes.
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PMID:Biomimetic dye affinity chromatography for the purification of bovine heart lactate dehydrogenase. 855 65