Hydrophobic chromatography of galactosyltransferase

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Abstract

O-Glycosidic analogs of N-acetylglucosamine are good substrates for galactosyltransferase, and as the O-substituted group becomes more hydrophobic, the apparent Km decreases as much as 2000-fold. l-leucine, leucine-amide, norleucine, valine, ε{lunate}-amino-n-caproic acid and tyrosine-agaroses all retain galactosyltransferase in the presence of 1.25 m ammonium sulfate. The enzyme is eluted quantitatively with a five- to tenfold purification by a decreasing linear gradient of ammonium sulfate. Galactosyltransferase was not specifically bound on any of a series of ω-aminoalkylagaroses tested. A simple and highly efficient procedure for the isolation of galactosyltransferase from bovine skim milk was developed and consisted of a 40-60% ammonium sulfate precipitation of the enzyme from skim milk followed by chromatography on (1) norleucine-Sepharose, (2) UDP-hexanolamine-Sepharose, and (3) α-lactalbumin-Sepharose. © 1976.

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APA

Geren, C. R., Magee, S. C., & Ebner, K. E. (1976). Hydrophobic chromatography of galactosyltransferase. Archives of Biochemistry and Biophysics, 172(1), 149–155. https://doi.org/10.1016/0003-9861(76)90060-6

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