The presence of a novel extracellular hyaluronidase in squid cranial cartilage.
A new type of hyaluronidase was isolated from squid cranial cartilage. The enzyme seems to be localised extracellularly, since it is extracted from the tissue by 0.5 M sodium acetate, pH 7.0, in the presence of proteinase inhibitors. Degradation studies suggest that the enzyme belongs to the family of endoglycosidases generating oligosaccharides of rather large size. The best activity of the enzyme was observed at pH 7.0 and 37 degrees C and the optimum buffer for digestion was 0.15 M Tris acetate. It is inactive in sodium phosphate, morpholine acetate and HEPES buffers. The enzyme degrades aggrecan, hyaluronan, chondroitin sulphate and oversulphated chondroitin sulphate.
Tsilemou
A
A
Laboratory of Biochemistry, Department of Chemistry, University of Patras, 26500 Patras, Greece.
Assouti
M
M
Papageorgakopoulou
N
N
Karamanos
N K
NK
Tsiganos
C P
CP
Vynios
D H
DH
D000818:Animals; D002356:Cartilage / Q000201:enzymology*; D002809:Chondroitin Sulfates / Q000378:metabolism; D049832:Decapodiformes / Q000201:enzymology*; D045604:Extracellular Fluid / Q000201:enzymology; D006821:Hyaluronoglucosaminidase / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D012886:Skull / Q000201:enzymology*
D002809:Chondroitin Sulfates; D006821:Hyaluronoglucosaminidase