Abstract
Rabbit cortical bone powder was extracted with EDTA solutions at neutral pH and the soluble constituents fractionated by DEAE-cellulose chromatography. The acidic fractions obtained were further investigated by gel chromatography and chemical analysis. Two classes of proteoglycans were present; one containing chondroitin sulphate and the other containing material resembling keratan sulphate mixed with a smaller amount of chondroitin sulphate. Sialoglycoproteins were detected by specific chemical introduction of tritium label into the sialic acid residues of the acidic glycoprotein fraction. Following sodium dodecyl sulphatepolyacrylamide gel electrophoresis and fluorography, the presence of numerous distinct sialoglycoprotein components was demonstrated.
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