Abstract
The chondroitin sulfate chain-initiating enzyme, UDP- d-xylose:core protein β- d-xylosyltransferase, has been purified from a high-speed supernatant fraction of a homogenate of embryonic chick cartilage by a procedure involving ammonium sulfate fractionation, gel chromatography on Sephadex G-200 resin, and affinity chromatography on a matrix consisting of core protein bound to Sepharose resin. The purified enzyme was homogeneous by electrophoretic and immunological criteria, had a molecular weight of 95,000–100,000 daltons, and was composed of two pairs of dissimilar subunits with molecular weights of ~23,000 and 27,000 daltons, respectively.
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