Assay of Glycoamidases and Endo-β-N-acetylglucosaminidases by Lectin Capture and Dissociation-Enhanced Lanthanide Fluorescence Immunoassay
作者： Ina L. Deras , Mutsumi Sano , Ikunoshin Kato , Yuan C. Lee
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摘要: Abstract We have developed an assay system for endo-β- N -acetylglucosaminidase and glycoamidase (PNGase), using Eu 3+ -labeled Man 9 GlcNAc 2 glycopeptides as substrates in combination with lectin capture. Two of different peptide lengths, derived from soybean agglutinin, were labeled via a diethylenetriaminepentaacetate (DTPA) chelating linker served two types enzymes: one (Man )Asn the other Ala-Ser-Phe-(Man )Asn-Phe-Thr activities. Following enzymatic hydrolysis, concanavalin A, immobilized or soluble, was added to mixture bind unreacted substrate unlabeled hydrolysis product. The product could then be separated lectin-bound complexes by filtration quantification dissociation-enhanced lanthanide fluorescence immunoassay. Activities low fmol min −1 rapidly quantified both enzymes, enzymological parameters determined within minutes. Applicability tested identification activity peak fractionation sweet almond emulsin, classic example. This offers sensitivity, ease use, high throughput. In addition, it is versatile should applicable glycobiology enzyme systems.
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