ω-Aminohexyl– Sepharose™ 4B is used mainly in affinity chromatography. It has been used in mitochondrial research to purify thioredoxin reductase (TrxR2), which is important in cell signaling and may also be an anticancer drug target.
Seminars in cancer biology, 16(6), 452-465 (2006-10-24)
Thioredoxin reductase (TrxR)-as part of a major thiol regulating system-allows redox metabolism to adjust to cellular requirements. Therefore, changes at the redox level reflect as a pars pro toto changes concerning the entire cell. Three different TrxR isoenzymes, TrxR1 as
The Journal of biological chemistry, 267(5), 3498-3505 (1992-02-15)
The chick kidney mitochondrial cytochrome P-450 1,25-dihydroxyvitamin D3 24-hydroxylase was partially purified by sequential polyethylene glycol precipitation, aminohexyl-Sepharose 4B, and hydroxylapatite chromatography. The specific activity of the final preparation, when reconstituted with NADPH, adrenodoxin, and adrenodoxin reductase, was 245 pmol/min/mg
The Journal of biological chemistry, 260(2), 1287-1289 (1985-01-25)
Bacterial luciferase from Vibrio harveyi, the 77,000-dalton light-emitting enzyme of the marine bacterium, has been crystallized into a two million cubic Angstrom cell with P212121 symmetry. The cell constants are a = 59.6 +/- 0.4 A, b = 112 +/-
Mitochondrial thioredoxin reductase (TrxR2) maintains thioredoxin (Trx2) in a reduced state and plays a critical role in mitochondrial and cellular functions. TrxR2 has been identified in many different tissues and can be purified to homogeneity from whole organs and isolated
The Journal of biological chemistry, 274(18), 12508-12516 (1999-04-23)
Actinomycin synthetase I (ACMS I) activates 4-methyl-3-hydroxyanthranilic acid, the precursor of the chromophoric moiety of the actinomycin, as adenylate. The gene acmA of ACMS I was identified upstream of the genes acmB and acmC encoding the two peptide synthetases ACMS
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