[35SO4] Dermatan sulfate, isolated from normal Hurler and Hunter fibroblasts was degraded by chondroitinase A, B, C to yield mono-and disaccharides. The products were separated by ion exchange chromatography and those arising from the non-reducing terminus were characterized by paper electrophoresis. The position of sulfate substituents was established by periodate oxidation and partial acid hydrolysis. Normal dermatan sulfate terminates with GalN-SO4 whereas IdUA-SO4 was a prominent terminus in Hunter dermatan sulfate but not in Hurler dermatan sulfate. It is concluded that Hunter's syndrome is due to a deficiency of L-idurono-sulfate sulfatase.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Oct 1 1973|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology