Concanavalin A binds of purified prolyl hydroxylase and partially inhibits its enzymic activity. Academic Article uri icon


  • Prolyl hydroxylase [(EC; prolyl-glycyl peptide, 2-oxoglutarate dioxygenase (4-hydroxylating)] was electrophoresed on polyacrylamide gels and the enzyme in the gels was shown to bind [acetyl-3H]concanavalin A. The enzyme-lectin complex was dissociated by treating the gel with methyl -D-mannopyranoside, a sugar known to inhibit binding of concanavalin A to glycoproteins. Furthermore, prolyl hydroxylase activity was partially inhibited by concanavalin A when the enzyme was assayed in the absence of bovine serum albumin, a protein which enhances enzymic activity. The inhibition of enzyme activity was prevented by sugars known to react with concanavalin A. 1976.

published proceedings

  • Biochem Biophys Res Commun

author list (cited authors)

  • Guzman, N. A., Berg, R. A., & Prockop, D. J.

citation count

  • 27

complete list of authors

  • Guzman, NA||Berg, RA||Prockop, DJ

publication date

  • January 1976