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. 1998 Jul 13;142(1):285–294. doi: 10.1083/jcb.142.1.285

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Characterization of polyclonal mouse antiserum against bovine collagen IX by ELISA and immunoblotting. (A) The antigens tested by ELISA were collagen IX (○), collagen XI (□), collagen II (▵), and decorin (⋄). (B) Noncollagenous proteins were extracted from chondroitinase ABC–digested pieces of bovine articular cartilage with boiling SDS-PAGE sample buffer containing 2% β-mercaptoethanol. Aliquots were electrophoresed on 4.5–15% polyacrylamide gels (lanes 1 and 4). Portions of a sample containing purified collagens II and XI were loaded in lanes 2 and 5. Pepsin-resistant collagen IX, i.e., the antigen, was applied in lanes 3 and 6. Proteins in the gel were stained with Coomassie Blue (lanes 1–3) or transferred to nitrocellulose and subjected to immunoblotting (lanes 4–6).

Characterization of polyclonal mouse antiserum against bovine collagen IX by ELISA and immunoblotting. (A) The antigens tested by ELISA were collagen IX (○), collagen XI (□), collagen II (▵), and decorin (⋄). (B) Noncollagenous proteins were extracted from chondroitinase ABC–digested pieces of bovine articular cartilage with boiling SDS-PAGE sample buffer containing 2% β-mercaptoethanol. Aliquots were electrophoresed on 4.5–15% polyacrylamide gels (lanes 1 and 4). Portions of a sample containing purified collagens II and XI were loaded in lanes 2 and 5. Pepsin-resistant collagen IX, i.e., the antigen, was applied in lanes 3 and 6. Proteins in the gel were stained with Coomassie Blue (lanes 1–3) or transferred to nitrocellulose and subjected to immunoblotting (lanes 4–6).