J. Biol. Chem., Vol. 259, Issue 19, 11771-11776, 10, 1984
Partial purification and characterization of 3'- phosphoadenylylsulfate:keratan sulfate sulfotransferases
ER Ruter and H Kresse
Two 3'-phosphoadenylylsulfate:keratan sulfate sulfotransferases were
purified 600-fold and 340-fold, respectively, from isolated bovine cornea
cells. Sulfotransferase I exhibited an apparent Mr = 220,000, whereas an Mr
= 140,000 was calculated for sulfotransferase II. The final preparations
were both devoid of chondroitin sulfate sulfotransferase activity. The
position of sulfation was determined by proton nuclear magnetic resonance
spectroscopy. Sixty per cent of the sulfate ester groups formed by
sulfotransferase I were linked to the C- 6 atom of galactosyl residues, the
other ones to the C-6 atom of N- acetylglucosamine. Sulfotransferase II
showed a different specificity: 23% of the newly formed sulfate ester
groups were on galactosyl and 77% on N-acetylglucosaminyl residues. Both
sulfotransferase preparations acted in a cooperative manner. In the
presence of both sulfotransferases, the incorporation of [35S]sulfate into
keratan sulfate was up to 75% higher than could be expected from the sum of
individual activities. From the specific radioactivities of the
oligosaccharides produced by digestion with endo-beta-galactosidase, it was
also concluded that both enzyme species reacted best with keratan sulfate
segments exhibiting a relatively high degree of sulfation.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
