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Updated: Jul 13, 2025

Respirometric Oxidative Phosphorylation Assessment in Saponin-permeabilized Cardiac Fibers
Published on: February 28, 2011
Effect of magnetic field modification on oxidative stability of myoglobin in sarcoplasm systems
Jingjiao Jiang1, Minquan Xia2, Honghong Gong1
1College of Life Science, Yangtze University, Jingzhou, Hubei 434023, PR China.
Abstract:
This study aimed to investigate the effect of magnetic fields (0, 3, 6, 12 mT) on the oxidation characteristics of myoglobin (Mb) in the sarcoplasmic protein (SP) system and to understander the underlying mechanism. The metmyoglobin content, Soret band of heme iron porphyrin, protein conformation and molecular weight distribution were measured in different Mb and SP samples. The results showed that the primary oxidation site of hydroxyl radical on Mb was likely to be the porphyrin ring structure and the side chain group of protein rather than the central iron atoms, what's more, 12 mT magnetic field treatment had an inhibitory effect on the oxidative damage induced by hydroxyl radical.
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