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

abstract

• Prolyl hydroxylase [(EC 1.14.11.2; 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

publisher

• Elsevier  Publisher

published in

• Biochemical and Biophysical Research Communications  Journal

keywords

• Animals
• Binding, Competitive
• Chick Embryo
• Concanavalin A
• Hexoses
• Kinetics
• Procollagen-Proline Dioxygenase

Digital Object Identifier (DOI)

• 10.1016/0006-291x(76)90704-x

start page

• 279

end page

• 285

volume

• 73

issue

• 2

URL

• http://dx.doi.org/10.1016/0006-291x(76)90704-x