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Nonconjugated Symmetrical Dienes
Published in George B. Butler, Cyclopolymerization and Cyclocopolymerization, 2020
Poly(dimethyldiallylammonium chloride), among other polyelectrolytes, was analyzed by size-exclusion chromatography, using Superose 6 gel packing.241 The elution curves showed no adsorptive affects for the polymers under appropriate ionic strength conditions.
Bio characterization of purified isoamylase from Rhizopus oryzae
Published in Preparative Biochemistry & Biotechnology, 2020
Banita Ghosh, Dibyajit Lahiri, Moupriya Nag, Sudipta Dash, Rina Rani Ray
It was observed that the result of purification of isoamylase from R. oryzaee PR7 (Table 1) that it had a specific activity of 8.93 U/mg. The process of ultrafiltration by the mechanism of Tangential Flow filtration was unable to improve the isoamylase activity to a considerable extent. But the enzyme showed 4.28 fold increase in its activity when it was passed through Superose 6 C-10/300GL column using the mechanism of size exclusion chromatography (Figure 1A). Isoamylase activity was detected in fractions eluted between 19th and 21st, which were pooled, concentrated and rechromatographed (Figure 1B).It was observed that the overall specific activity of purified was increased by 5.87 times to 52.4 U/mg (mM/min/mg).Although purification of isoamylase in previous studies involved various methods like raw starch adsorption-desorption,[2] gel electrophoresis and low speed sedimentation,[4] ultracentrifugation and disc gel electrophoresis,[13] gel filtration,[3,14] affinity chromatography,[5] and combinations of ion-exchange and gel filtration chromatography[15,16] the present study employed a simple purification strategy involving filtration and size exclusion chromatographic technique only.
Factors affecting therapeutic protein purity and yield during chromatographic purification
Published in Preparative Biochemistry & Biotechnology, 2023
Che Haznie Ayu Che Hussian, Wai Yie Leong
Proteins must be adapted to the buffer environment during elution; hence the selection of the mobile phase is essential for the purification of proteins. Size exclusion chromatography with Superose 12 was used in research with four different mobile phases (tris, acetate, phosphate, and sulfate) at pH 7.2.[78] Using mobile phase buffers of tris, acetate, phosphate, and sulfate, recovery yields of rhAT of 50, 52, 54, and 51 percent and purities of 97, 98, 98, and 97 were achieved. This clarified how phosphate buffer was able to get a high recovery yield (54%) with a 98% purity.