The effect of zwitterionic detergents on the extraction and functional properties of cartilage proteoglycans.

A range of structurally related zwitterionic detergents, Zwittergents 3-06, 3-08, 3-10, and 3-12, and a derivative of cholic acid (Chaps) were examined for their ability to enhance the extraction of newly synthesized, intracellular proteoglycans and for their effect on the functional properties of cartilage proteoglycan. Although none of the detergents could extract greater than 4% of the intracellular proteoglycans when used alone, Zwittergents 3-10, 3-12, and Chaps proved equally as effective when used in combination with 4 M guanidine HCl extracting greater than 90% of newly synthesized proteoglycans. Rate zonal centrifugation of aggregates containing either 3H-link protein or 3H-monomer, which had been incubated with 2% (w/v) detergent indicated that none of the test detergents caused a disassembly of intact aggregates. However, both Zwittergents 3-10 and 3-12 prevented the reaggregation of components dissociated with 4 M guanidine HCl. Similar to the finding with aggregate, none of the detergents caused a disassembly of monomer-link protein complexes prepared from purified 3H-link protein and proteoglycan monomer, while Zwittergents 3-10 and 3-12 prevented their assembly from free link protein and monomer. However, monomer-link protein complexes once formed were able to associate with hyaluronic acid to form link-stable ternary complexes in the presence of all detergents tested including Zwittergents 3-10 and 3-12.