Purification of chondroitin 6-sulfotransferase secreted from cultured chick embryo chondrocytes.

@article{Habuchi1993PurificationOC,
  title={Purification of chondroitin 6-sulfotransferase secreted from cultured chick embryo chondrocytes.},
  author={Osami Habuchi and Yasushi Matsui and Y Kotoya and Yuri Aoyama and Yuichi Yasuda and M. T. Noda},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 29},
  pages={21968-74}
}
Chondroitin 6-sulfotransferase, which transfers sulfate from 3'-phosphoadenylyl sulfate to position 6 of N-acetylgalactosamine in chondroitin, was purified 1,430-fold to apparent homogeneity with a 22% yield from the serum-free culture medium of chick embryo chondrocytes by affinity chromatography on heparin-Sepharose CL-6B, wheat germ agglutinin-agarose, and 3',5'-ADP-agarose. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme showed a single broad protein band… CONTINUE READING
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