Analysis of Nitrosyl hemoglobin by Electron paramagnetic resonance (EPR) spectroscopy (CAT#: STEM-MB-1048-WXH)

Name: Analysis of Nitrosyl hemoglobin by Electron paramagnetic resonance (EPR) spectroscopy
SKU: STEM-MB-1048-WXH
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Introduction

Nitrosyl hemoglobin is relatively stable under aerobic conditions and under- goes reversible O2 binding at the heme sites of its -sub- units. Its O2 binding is coupled to the structural/func- tional transition between T- (low affinity extreme) and R- (high affinity) states.

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Principle Applications Procedure Materials

Principle

Electron Paramagnetic Resonance (EPR), also called Electron Spin Resonance (ESR), is a branch of magnetic resonance spectroscopy which utilizes microwave radiation to probe species with unpaired electrons, such as radicals, radical cations, and triplets in the presence of an externally applied static magnetic field.
EPR spectroscopy is particularly suitable for the investigation of (bio)chemical systems with strongly localized spin density and their interaction with the environment. For these systems EPR provides information on the structure and dynamics and is widely used in chemistry, physics and biology.

Applications

• Study dynamic organisation of lipids in biological membranes, lipid-protein interactions and temperature of transition of gel to liquid crystalline phases.
• Determine oxygen levels in tissues and blood.
• Injection of spin-labeled molecules allows for electron resonance imaging of living organisms.
• EPR can be used to measure microviscosity and micropolarity within drug delivery systems as well as the characterization of colloidal drug carriers.
• The study of radiation-induced free radicals in biological substances (for cancer research).
• Investigation on the antioxidant properties of medicine