J Med Microbiol Email Content Delivery
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Shain, H.
Right arrow Articles by Beighton, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shain, H.
Right arrow Articles by Beighton, D.
Agricola
Right arrow Articles by Shain, H.
Right arrow Articles by Beighton, D.

The Journal of Medical Microbiology, Vol 44, Issue 5 381-389, Copyright © 1996 by Society for General Microbiology

JOURNAL ARTICLE

Purification and properties of a novel glycosaminoglycan depolymerase from Streptococcus intermedius strain UNS 35

H. Shain, K. A. Homer and D. Beighton
Joint Microbiology Research Unit, King's College School of Medicine and Dentistry, London, UK.

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. 83000. 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 pI of approximately 9.3.


This article has been cited by other articles:


Home page
 MicrobiologyHome page
D. Pecharki, F. C. Petersen, and A. Aa. Scheie
Role of hyaluronidase in Streptococcus intermedius biofilm
Microbiology, March 1, 2008; 154(3): 932 - 938.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL J MED MICROBIOL MICROBIOLOGY J GEN VIROL ALL SGM JOURNALS
Copyright © 1996 Society for General Microbiology.