%0 Journal Article %A Shain, H. %A Homer, K. A. %A Beighton, D. %T Purification and properties of a novel glycosaminoglycan depolymerase from Streptococcus intermedius strain UNS 35 %D 1996 %J Journal of Medical Microbiology, %V 44 %N 5 %P 381-389 %@ 1473-5644 %R https://doi.org/10.1099/00222615-44-5-381 %I Microbiology Society, %X A glycosaminoglycan (GAG) depolymerase that acts on chondroitin sulphate A (CS-A), chondroitin sulphate C (CS-C) and hyaluronic acid (HA) was purified to apparent homogeneity from a culture of Streptococcus intermedius, strain UNS 35, grown in minimal medium supplemented with CS-A as the sole carbon source. The enzyme was purified by ammonium sulphate precipitation followed by serial chromatography on DEAE Trisacryl M, CM Trisacryl M and heparin-agarose. SDS-PAGE analysis of the purified enzyme yielded a single band with a mol. wt of c. 83 000. The purified GAG depolymerase was unusual in its substrate specificity. The enzyme was initially regarded as a CS depolymerase because of its induction by CS-A. However, the GAG depolymerase exhibited greatest activity against HA, whereas the degradation rates of CS-A and CS-C were c. 8% and 2%, respectively, of the rate with HA. On this basis the enzyme could be classified as a hyaluronidase rather than a CS depolymerase. The pH optimum was around neutrality and the enzyme was unusual in having a high pl of approximately 9.3. %U https://www.microbiologyresearch.org/content/journal/jmm/10.1099/00222615-44-5-381