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JBC, Vol. 252, Issue 6, 1980-1989, Mar, 1977
Polydispersity of cartilage proteoglycans. Structural variations with size and buoyant density of the molecules
D. Heinegard
Proteoglycan monomers were subfractionated according to buoyant density by
dissociative CsCl density gradient centrifugation. It was shown that with
decreasing buoyant density of the proteoglycan subfraction: (a) the average
sizes of the molecules decreased (shown by Sepharose 2B chromatography);
(b) the relative content of chondroitin sulfate decreased; (c) the relative
content of protein increased; (d) the relative proportion of the amino
acids glycine and serine, which occur close to the chondroitin
sulfate-peptide linkage, decreased; (e) the relative proportion of the
hyaluronic acid-binding region released by treatment of proteoglycans with
cyanogen bromide increased; (f) the relative content of the keratan
sulfate-enriched region increased. The data indicate that proteoglycans
contain a nonvariable hyaluronic acid-binding region, a keratan
sulfate-enriched region and a chondroitin sulfate-enriched region of
variable size. It is concluded that proteoglycans vary in size mainly
because of variations in the size of the chondroitin sulfate-enriched
region. Additional data were obtained using subfractions of proteoglycan
monomers isolated according to size differences by using Sepharose 2B
chromatography. The Kav values of the subfractions on Sepharose 2B ranged
from 0 to 0.54. Analyses of these subfractions showed the same variations
with size of the content of chondroitin sulfate, protein, amino acids,
hyaluronic acid-binding region, and keratan sulfate-enriched region, as was
shown for the subfractions isolated at different buoyant densities in the
dissociative gradient.

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Copyright © 1977 by the American Society for Biochemistry and Molecular Biology.
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