Purification and properties of bacterial chondroitinases and chondrosulfatases.

  title={Purification and properties of bacterial chondroitinases and chondrosulfatases.},
  author={Tatsuya Yamagata and Hiroyuki Saito and Osami Habuchi and Sakura Suzuki},
  journal={The Journal of biological chemistry},
  volume={243 7},
1. An enzyme, “chondroitinase-ABC,” has been purified to apparent homogeneity from extracts of Proteus vulgaris, NCTC 4636, which was adapted on a medium containing chondroitin sulfate C. It has the following properties. (a) At pH 8, it degrades chondroitin sulfates A, B, and C at greater rates than chondroitin and hyaluronic acid. It does not attack keratosulfate, heparin, or heparitin sulfate. (b) It carries out an elimination reaction, yielding A4,5-unsaturated disaccharides. (c) In the… CONTINUE READING
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