Primary structure of tetranectin, a plasminogen kringle 4 binding plasma protein: homology with asialoglycoprotein receptors and cartilage proteoglycan core protein

Tetranectin binds to plasminogen and to isolated kringle 4 [Clemmensen, I., Petersen, L. C., & Kluft, C. (1986) Eur. J. Biochem. 156, 327-333], apparently to its lysine-binding site. Each of the four identical chains consists of 181 amino acid residues. The three intrachain disulfide bonds connect Cys residues 50-60, 77-176, and 152-168. The tetranectin sequence is homologous (17-24% identical positions) with those parts of the...