PMID: 2603Feb 25, 1976

Chondroitinase C from Flavobacterium heparinum.

The Journal of Biological Chemistry
Yara M Michelacci, C P Dietrich

Abstract

A chondroitinase that acts upon chondroitin sulfate C and hyaluronic acid was isolated from Flavobacterium heparinum. This enzyme was seperated from constitutional chondroitinase AC and an induced chondroitinase B also present in extracts of F. heparinum previously grown in the presence of chondroitin sulfates A, B or C. The enzyme acts upon chondroitin sulfate C producing tetrasaccharide plus an unsaturated 6-sulfated disaccharide (delta Di-6S), and upon hyaluronic acid producing unsaturated nonsulfated disaccharide (delta Di-OS). Chondroitin sulfate A is also degraded producing oligosaccharides and delta Di-6S but not delta Di-4S. The chondroitinase C is also distinguished from the chondroitinases B and AC by several properties, such as effect of ions, temperature for optimal activity, and susceptibility to increasing salt concentrations. The substrate specificity of the chondroitinase C is different from that of any other chondroitinase or hyaluronidase described so far.

Related Concepts

Chondroitin Sulfate, Zinc Salt
Chondroitinases
Disaccharides
Flavobacterium genus
Hydrogen-Ion Concentration
Kinetics
Osmolality
Orthophosphate
Sodium Chloride, (24)NaCl
Structure-Activity Relationship

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