Subunit structure of bovine ESF (extracellular‐matrix stabilizing factor(s))

Two chondroitin sulfate-containing complexes have been isolated from fetal bovine serum and shown to contain the serine protease inhibitor bikunin. A complex of 126 kDa contains bikunin linked by a chondroitin sulfate chain to a protein with homology to the HC2 component of the human inter-alpha-trypsin inhibitor. This complex represents the extracellular matrix stabilizing factor recently described as a bikunin-containing fraction necessary for expansion of the cumulus matrix [(1992) J. Biol. Chem. 267, 12380-12386]. A second complex of 236 kDa contains, in addition to bikunin and HC2, a bovine homolog of HC3 of the human pre-alpha-trypsin inhibitor. Thus, bovine bikunin is a chondroitin sulfate proteoglycan that achieves multifunctionality by linkage to proteins homologous to human serine antiproteinase complexes.