PubMed · 5130833
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R K Joshi, L Krasnec, I Lacko. 1971. Studies on solubilization. II.. https://pubmed.ncbi.nlm.nih.gov/5130833/
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The application of a purification procedure for the industrial preparation from human plasma of a therapeutic protein may be hindered by several safety concerns. The dye leaching from Remazol Yellow GGL-Sepharose used for the affinity chromatography of human plasma transthyretin was quantitatively studied by a sensitive competitive enzyme immunoassay. The possibility of including a heat treatment step for virus inactivation in the purification process while preserving the biochemical and functional characteristics of the protein is also reported.
Two azoreductases (I and II) were purified to homogeneity from extracts of Shigella dysenteriae (type 1). Azoreductase I was a dimer of identical subunits of M(r) 28,000, whereas azoreductase II was a monomer of 11,000 M(r). Both were flavoproteins, each containing 1 mol of FMN per mol enzyme. Both NADH and NADPH functioned as electron donors for the azoreductases. Azoreductase I used Ponceau SX, Tartrazine, Amaranth and Orange II as substrates. Azoreductase II utilized all the dyes except Amaranth.
The results of experiments testing the effects of yeasts, sunlight, and temperature on the food dyes tartrazine, ponceau 4R, indigotin and azorubin (used for colouring ginger soft drink) are reported. Light was found to exert a greater influence than heat, and yeasts growth hastened colour degradation. Yeasts assimilated to varying extent the colouring compounds and, when failing to do it, showed a certain power of adsorption by the no longer viable cells.