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Glycomacropeptide (GMP) was purified from sweet whey dialyzed in water by anion-exchange chromatography on DEAE-Sephacel at pH 2.0–4.5. The optimum pH range was 2.5–4.0. The yield of purified GMP increased and its sialic acid concentration decreased with increasing pH value. The GMP had an apparent isoelectric point < 3.8. Dialysis of sweet whey was shown to be important to maximize the yield of...
Glycomacropeptide (GMP) was purified from non-dialyzable fraction of sweet whey by anion-exchange chromatography on DEAE-Sephacel at two pHs 6.4 and 3.0. Chromatography at pH 3.0 (but not pH 6.4) gave a GMP fraction of high purity with its yield (1 g from every litre of whey) being approximately 100 times higher than that shown in the previous report. It was concluded that DEAE-Sephacel chromatography...
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