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Related Concept Videos

Hemoglobin01:24

Hemoglobin

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...

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Antigens Protected Functional Red Blood Cells By The Membrane Grafting Of Compact Hyperbranched Polyglycerols
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Electron-transfer reactivity and enzymatic activity of hemoglobin in a SP Sephadex membrane.

C Fan1, H Wang, S Sun

  • 1Department of Biochemistry and National Laboratory of Pharmaceutical Biotechnology, Nanjing University, PR China.

Analytical Chemistry
|July 27, 2001
PubMed
Summary

Hemoglobin entrapped in SP Sephadex membranes shows direct electron transfer and enhanced peroxidase activity. This enables the development of a sensitive biosensor for detecting hydrogen peroxide (H2O2).

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Area of Science:

  • Electrochemistry
  • Biochemistry
  • Biosensor Technology

Background:

  • Hemoglobin (Hb) is crucial for oxygen transport but also possesses enzymatic activity.
  • Modifying electrode surfaces with biomolecules can create novel biosensors.
  • SP Sephadex membranes offer a suitable matrix for immobilizing proteins.

Purpose of the Study:

  • To investigate the electrochemical properties of hemoglobin immobilized in an SP Sephadex membrane.
  • To evaluate the enhanced peroxidase activity of hemoglobin within the SP Sephadex matrix.
  • To develop a biosensor for hydrogen peroxide (H2O2) detection based on these properties.

Main Methods:

  • Immobilization of hemoglobin (Hb) within an SP Sephadex membrane on a pyrolytic graphite electrode.
  • Electrochemical characterization using cyclic voltammetry to determine redox properties.
  • Enzymatic activity assay to measure peroxidase activity and determine kinetic parameters (Michaelis-Menten constant).
  • Fabrication and testing of a Hb/SP Sephadex membrane-based H2O2 biosensor.

Main Results:

  • Stable and well-defined redox waves observed for Hb in the SP Sephadex membrane at specific potentials (-0.244 V anodic, -0.336 V cathodic vs SCE).
  • Significantly enhanced peroxidase activity of Hb within the membrane, with a low apparent Michaelis-Menten constant (1.9 mM).
  • Successful development of a H2O2 biosensor with a linear detection range from 5.0 x 10(-6) to 1.6 x 10(-4) mol/L.

Conclusions:

  • Hemoglobin immobilized in SP Sephadex membranes exhibits direct electron transfer and enhanced enzymatic activity.
  • The Hb/SP Sephadex modified electrode is effective for the electrochemical sensing of hydrogen peroxide.
  • This approach offers a promising platform for developing sensitive and stable H2O2 biosensors.