1. 1. A chondroitin sulfate proteogylcan was isolated from leukocyte granules and partly characterized. It had a low protein content and a relatively low molecular size. 2. 2. The incorporation of [35S]sulfate, [14C]glucosamine and [3H]serine into chondroitin sulfate was inhibited by puromycin, indicating that the elongation of the polysaccharide chain is dependent on prior synthesis of protein. 3. 3. [14C]Serine incorporated into the chondroitin sulfate was destroyed with alkali by a β-elimination reaction, indicating that the polysaccharide is covalently linked to the hydroxyl of serine. 4. 4. Gel-chromatography of the 35-labeled polysaccharide isolated from sub-cellular fraction indicated that chondroitin sulfate is synthesized as a proteoglycan on microsomal structures. © 1969.