Monoclonal antibodies recognizing protease-generated neoepitopes from cartilage proteoglycan degradation : application to studies of human link protein cleavage by stromelysin
Monoclonal antibodies were raised that specifically recognize the NH2-terminal neoepitope sequence present in like protein cleavage products derived from stromelysin-degraded proteoglycan aggregate. Competitive enzyme-linked immunosorbend assay, using synthetic peptides as inhibitors, showed that one of these antibodies (CH-3) required, for antibody recognition, the free NH2-terminal amino acid isoleucine (residue 17 of the intact protein) in the sequence NH2-IQAENG at the stromelysin cleavage site of link protein 3.Monoclonal antibodies were raised that specifically recognize the NH2-terminal neoepitope sequence present in like protein cleavage products derived from stromelysin-degraded proteoglycan aggregate. Competitive enzyme-linked immunosorbend assay, using synthetic peptides as inhibitors, showed that one of these antibodies (CH-3) required, for antibody recognition, the free NH2-terminal amino acid isoleucine (residue 17 of the intact protein) in the sequence NH2-IQAENG at the stromelysin cleavage site of link protein 3
