Covalent Linkage between Proteins of the Inter-α-inhibitor Family and Hyaluronic Acid Is Mediated by a Factor Produced by Granulosa Cells

This publication has 20 references indexed in Scilit:

• Chondroitin sulphate covalently cross‐links the three polypeptide chains of inter‐α‐trypsin inhibitor
  European Journal of Biochemistry, 1994
• In vivoBinding of Human Inter-α-Trypsin Inhibitor Free Heavy Chains to Hyaluronic Acid
  Biological Chemistry Hoppe-Seyler, 1994
• Presence of the protein-glycosaminoglycan-protein covalent cross-link in the inter-alpha-inhibitor-related proteinase inhibitor heavy chain 2/bikunin.
  Published by Elsevier ,1993
• Subunit structure of bovine ESF (extracellular‐matrix stabilizing factor(s))
  FEBS Letters, 1993
• Functional significance of cumulus expansion in the mouse: Roles for the preovulatory synthesis of hyaluronic acid within the cumulus mass
  Molecular Reproduction and Development, 1993
• Hyaluronic acid synthesis and gap junction endocytosis are necessary for normal expansion of the cumulus mass
  Molecular Reproduction and Development, 1990
• Binding of haptoglobin, inter-alpha-trypsin inhibitor, and alpha 1 proteinase inhibitor to synovial fluid hyaluronate and the influence of these proteins on its degradation by oxygen derived free radicals.
  Annals of the Rheumatic Diseases, 1988
• Carbohydrate as covalent crosslink in human inter‐α‐trypsin inhibitor: A novel plasma protein structure
  FEBS Letters, 1988
• Isolation and characterization of cDNAs encoding the heavy chain of human inter-alpha-trypsin inhibitor (I alpha TI): unambiguous evidence for multipolypeptide chain structure of I alpha TI.
  Proceedings of the National Academy of Sciences, 1987
• Ovulation and the mechanism of follicle rupture
  Cell and tissue research, 1974