The fluorescence emission of the apo-glucose oxidase from Aspergillus niger as probe to estimate glucose concentrations

被引：61

作者：

D'Auria, S

Herman, P

Rossi, M

Lakowicz, JR

机构：

[1] Univ Maryland, Sch Med, Dept Biochem & Mol Biol, Ctr Fluorescence Spect, Baltimore, MD 21201 USA

[2] CNR, Inst Prot Biochem & Enzymol, I-80125 Naples 10, Italy

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1999年 / 263卷 / 02期

关键词：

glucose oxidase; fluorescence spectroscopy; glucose estimation; diabetes; time-resolved fluorescence;

D O I：

10.1006/bbrc.1999.1330

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We developed a new method of glucose sensing using an inactive form of glucose oxidase from Aspergillus niger. Glucose oxidase was rendered inactive by removal of the FAD cofactor. The resulting ape-glucose oxidase still binds glucose as observed from a decrease in its intrinsic tryptophan fluorescence. 8-Anilino-1-naphthalenesulfonic acid (ANS) was found to bind spontaneously to ape-glucose oxidase as seen from an enhancement of the ANS fluorescence. The steady state intensity of the bound ANS decreased 25% upon binding of glucose, and the mean lifetime of the bound ANS decreased about 40%. These spectral changes occurred with a midpoint from 10 to 20 mM glucose, which is comparable to the KD of hole-glucose oxidase. These results suggest that ape-glucose oxidase can be used as a reversible nonconsuming sensor for glucose. (C) 1999 Academic Press.

引用

收藏

页码：550 / 553

页数：4

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