Concanavalin A binds of purified prolyl hydroxylase and partially inhibits its enzymic activity. |
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Authors: | N A Guzman R A Berg D J Prockop |
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Institution: | Department of Biochemistry, College of Medicine and Dentistry of New Jersey Rutgers Medical School, Piscataway, New Jersey 08854 USA |
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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 α-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. |
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