Type XI collagen (1 alpha 2 alpha 3 alpha) extracted from bovine articular cartilage by pepsin digestion binds strongly to heparin immobilized on agarose. The collagens from cartilage will bind to heparin-agarose in 0.1 M NaCl/2 M urea/0.01 M Tris-HCl and can be eluted with a linear gradient of NaCl. Type XI begins to elute at NaCl concentrations higher than 0.28 M and is totally eluted at 0.40 M NaCl. The peak of elution occurs at 0.37 M NaCl. The other collagens of cartilage bind more weakly and are fully eluted when the NaCl concentration reaches 0.25 M. Collagen types I, III, and V are also bound to the column at low salt concentrations but are fully eluted before type XI begins to elute. All of the type XI preparation binds to heparin-agarose, suggesting that there is at least one binding site per molecule. Denatured 1 alpha and 2 alpha chains bind strongly, suggesting that at least one binding site exists on both of these chains. These data confirm that the interaction between polyanions and type XI collagen is stronger than that with other known collagens and provide a method for purification of type XI without any type II contamination.