Direct enzyme-substrate affinity determination by real-time hyperpolarized 13C-MRS

被引：2

作者：

Friesen-Waldner, L. J. ^{[1
]}

Wiens, C. N. ^{[1
]}

Wade, T. P. ^{[1
]}

Thind, K. ^{[1
]}

Sinclair, K. P. ^{[1
]}

Hovav, Y. ^{[2
]}

Gomori, J. M. ^{[3
]}

Sosna, J. ^{[3
]}

McKenzie, C. A. ^{[1
]}

Katz-Brull, R. ^{[3
]}

机构：

[1] Univ Western Ontario, Dept Med Biophys, London, ON, Canada

[2] Weizmann Inst Sci, IL-76100 Rehovot, Israel

[3] Hadassah Hebrew Univ Med Ctr, Dept Radiol, Jerusalem, Israel

来源：

CHEMICAL COMMUNICATIONS | 2014年 / 50卷 / 89期

基金：

以色列科学基金会; 欧洲研究理事会;

关键词：

CHOLINE-OXIDASE; BETAINE-ALDEHYDE; GLYCINE BETAINE; OXIDATION; KINETICS;

D O I：

10.1039/c4cc05418k

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A specialized kinetic analysis of real-time hyperpolarized [1,1,2,2-D-4, 1-C-13] choline C-13-magnetic resonance spectroscopy enabled the determination of initial rates of metabolic enzyme activity (choline oxidase), enzyme-substrate affinity (K-m), and inhibition. In a clinical MRI scanner, metabolite levels lower than 16 mu M were detected at a temporal resolution of 1 s.

引用

页码：13801 / 13804

页数：4

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