Immobilized Enzymes and Cells Part D by Nathan P. Colowick, Nathan P. Kaplan, Klaus Mosbach

By Nathan P. Colowick, Nathan P. Kaplan, Klaus Mosbach

The severely acclaimed laboratory general, Methods in Enzymology , is among the so much hugely revered courses within the box of biochemistry. considering the fact that 1955, each one quantity has been eagerly awaited, often consulted, and praised by way of researchers and reviewers alike. The sequence includes a lot fabric nonetheless appropriate this present day - actually an important book for researchers in all fields of existence sciences.

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Extra resources for Immobilized Enzymes and Cells Part D

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A. 70, 2534 (1973). ~7 M. Hikuma and T. Yasuda [10], I. K a r u b e [11], and F. S c h u b e r t and F. W. Scheller [13], this volume.

The sensitivity for maltose in comparison to glucose is about 50%. This decreased signal might be caused by the approximately doubled diffusional resistance of the membrane to maltose owing to its larger molecular cross section. The linear range extends up to 2 mM maltose. 1), splits starch into maltose via dextrin fragments. These products are indicated by the glucoamylaseGOD electrode. 0, is pipetted into the measuring cell and equilibrated at 37°. When a constant baseline is reached, the reaction is started by addition of 100 txl of serum.

0, containing variable amounts of NADH (Fig. 8). The electrode is polarized to -600 mV. The glucose sample is added after attaining a constant baseline. An amplification factor of 8 is obtained in the solution containing 10 mM cofactor. 8 /~M glucose. Amplification makes use of a part of the GOD excess which is unused in the absence of NADH. The overall reaction represents the oxidation of NADH by oxygen, with glucose acting as the mediator between the two enzymes. Enzyme Competition The problem of measuring cofactor concentrations with electrochemical sensors may be solved if a cofactor-dependent enzyme is coupled with an oxidase, with both competing for the same substrate.

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