Demonstration of an endo-beta-galactosidase and an endo-beta-xylosidase that degrade the proteoglycan linkage region.
Purified proteochondroitin sulfate was incubated at pH 4.0 with a rabbit liver lysosomal enzyme fraction. The formed degradation products were isolated by gel filtration followed by reduction with NaB3H4. After acid hydrolysis of the reduced digest, the hydrolysate was passed through Dowex 50W-X8 and 1-X2 columns. The separated neutral sugars were then subjected to paper chromatography, which demonstrated that galactose and xylose had been at the reducing termini of chondroitin sulfate after incubation with the liver lysosomal preparation. These results suggest the presence in the liver lysosomal preparation of an endo-beta-galactosidase and an endo-beta-xylosidase which act at the linkage region of proteochondroitin sulfate.
D000818:Animals; D002850:Chromatography, Gel; D002854:Chromatography, Paper; D005696:Galactosidases / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008297:Male; D011509:Proteoglycans / Q000378:metabolism*; D011817:Rabbits; D013997:Time Factors; D014995:Xylosidases / Q000032:analysis / Q000378:metabolism*; D001616:beta-Galactosidase / Q000032:analysis / Q000378:metabolism*
D011509:Proteoglycans; D005696:Galactosidases; D006026:Glycoside Hydrolases; D014995:Xylosidases; C056547:endo-beta-xylosidase; C026093:keratan-sulfate endo-1,4-beta-galactosidase; D001616:beta-Galactosidase