PMID: 2492437Jan 27, 1989Paper

Lectin affinity bioassay: an assay method for glycoprotein enzyme

Biochimica Et Biophysica Acta
A Electricwala

Abstract

A simple and sensitive chromogenic microtitre plate assay for glycoprotein enzymes is described, using melanoma tissue plasminogen activator (t-PA) as a model enzyme. The assay is based on the binding of t-PA to immobilised lectin and quantitating the bound enzyme with plasminogen, fibrinogen fragments and chromogenic substrate S-2251 on an ELISA plate reader. Seven different lectins were examined for the binding of t-PA, and of these, concanavalin A was chosen for subsequent studies. The specificity of this binding can be inhibited dose-dependently in the presence of D-mannose and methyl alpha-D-mannoside, but not by D-glucose and D-lactose. The lower limit of the sensitivity of this assay is about 0.5 IU/ml. Comparison of the dose-response curves indicates that the sensitivity of this assay method is very similar to that of bioimmunoassay using anti-t-PA IgG to capture the antigen. The applicability of this method to other glycoprotein enzymes was also evaluated using alkaline phosphatase from bovine mucosa. The specificity of this method was related to the choice of substrate and this was shown by analysis of a mixture of t-PA and alkaline phosphatase. It is suggested that this assay can be adapted for the analysis of comple...Continue Reading

References

Feb 15, 1986·Thrombosis Research·C KorningerB R Binder
Jun 1, 1986·Proceedings of the Society for Experimental Biology and Medicine·G OpdenakkerP De Somer
Jan 1, 1985·Annual Review of Biochemistry·R Kornfeld, S Kornfeld
Sep 29, 1972·Biochimica Et Biophysica Acta·M L DufauK J Catt
Sep 15, 1982·Thrombosis Research·M RånbyP Wallén

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Citations

Dec 9, 2004·Chemical Reviews·Raz Jelinek, Sofiya Kolusheva

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