Abstract
A particulate enzyme preparation from embryonic chick cartilage catalyzes incorporation of radioactivity from UDP-GalNAc- 3H or UDP-Glc-UA- 14C into chondroitin sulfate. In the absence of added oligosaccharide acceptor, incorporation of radioactivity from either nucleotide required the presence of the alternate unlabeled nucleotide. Addition of a sulfated or nonsulfated hexasaccharide derived from chondroitin sulfate (nonreducing terminal glcUA) stimulated incorporation of radioactivity from UDP-GalNAc- 3H in the absence of UDP-GlcUA, but not from UDP-GlcUA- 14C in the absence of UDP-GalNAc. In contrast, the addition of nonsulfated pentasaccharide (nonreducing terminal galNAc) did not stimulate the incorporation of radioactivity from UDP-GalNAc- 3H in the absence of UDP-GlcUA, but did stimulate incorporation of radioactivity from UDP-GlcUA- 14C in the absence of UDP-GalNAc. The radioactive product of this reaction was characterized as a nonsulfated hexasaccharide with a radioactive nonreducing terminal glcUA. The sulfated pentasaccharide did not accept glcUA- 14C or galNAc- 3H from the appropropriate nucleotide.
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