Co-purification and characterization of UDP-glucose 4-epimerase and UDP-N-acetylglucosamine 4-epimerase from porcine submaxillary glands.

@article{Piller1983CopurificationAC,
  title={Co-purification and characterization of UDP-glucose 4-epimerase and UDP-N-acetylglucosamine 4-epimerase from porcine submaxillary glands.},
  author={Friedrich Piller and Mary H. Hanlon and Robert Frederick lll Hill},
  journal={The Journal of biological chemistry},
  year={1983},
  volume={258 17},
  pages={
          10774-8
        }
}
UDP-glucose 4-epimerase and UDP-N-acetylglucosamine 4-epimerase have been co-purified about 9,000-fold from porcine submaxillary glands by affinity chromatography on UDP-hexanolamine-agarose. The homogeneous epimerase has apparent Mr = 88,000 and contains two subunit species with apparent Mr = 37,000 and 35,000, respectively. The two subunits, however, are indistinguishable as judged by peptide mapping. The purified enzyme catalyzes equally well the reversible reactions UDP-glucose in… CONTINUE READING

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