Muhan Zhang1,2, Daoying Wang2, Xinglian Xu1, Weimin Xu2. 1. Key Lab of Meat Processing and Quality Control, Ministry of Education, Nanjing Agricultural University, Nanjing 210095, China. 2. Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China.
Abstract
OBJECTIVE: The objectives of this study were to investigate the direct antioxidative effect of 90 Kda heat shock protein (Hsp90) obtained from duck muscle. METHODS: The interaction of Hsp90 with phospholipids and oxidized phospholipids was studied with surface plasmon resonance (SPR), and their further oxidation in the presence of Hsp90 was evaluated with thiobarbituric acid reactive substances (TBARS) assay. The scavenging effect on the 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid (ABTS) was measured, and the electron paramagnetic resonance (EPR) spectroscopy in combination with 5-tert-Butoxycarbonyl-5-methyl-1-pyrroline-N-oxide and 2-phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide (PTIO) was utilized to determine the abilities of Hsp90 in scavenging hydroxyl and PTIO radicals. RESULTS: SPR showed Hsp90 could bind with both phospholipids and oxidized phospholipids, and prevent their further oxidation by the TBARS assay. The DPPH and ABTS scavenging activity increased with Hsp90 concentration, and could reach 27% and 20% respectively at the protein concentration of 50 μM. The EPR spectra demonstrated Hsp90 could directly scavenge ·OH and PTIO· radicals. CONCLUSION: This suggests that Hsp90, a natural antioxidant in meat, may play an important role in cellular defense against oxidative stress, and may have potential use in meat products.
OBJECTIVE: The objectives of this study were to investigate the direct antioxidative effect of 90 Kda heat shock protein (Hsp90) obtained from duck muscle. METHODS: The interaction of Hsp90 with phospholipids and oxidized phospholipids was studied with surface plasmon resonance (SPR), and their further oxidation in the presence of Hsp90 was evaluated with thiobarbituric acid reactive substances (TBARS) assay. The scavenging effect on the 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid (ABTS) was measured, and the electron paramagnetic resonance (EPR) spectroscopy in combination with 5-tert-Butoxycarbonyl-5-methyl-1-pyrroline-N-oxide and 2-phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide (PTIO) was utilized to determine the abilities of Hsp90 in scavenging hydroxyl and PTIO radicals. RESULTS: SPR showed Hsp90 could bind with both phospholipids and oxidized phospholipids, and prevent their further oxidation by the TBARS assay. The DPPH and ABTS scavenging activity increased with Hsp90 concentration, and could reach 27% and 20% respectively at the protein concentration of 50 μM. The EPR spectra demonstrated Hsp90 could directly scavenge ·OH and PTIO· radicals. CONCLUSION: This suggests that Hsp90, a natural antioxidant in meat, may play an important role in cellular defense against oxidative stress, and may have potential use in meat products.
Entities:
Keywords:
90 Kda heat shock protein (Hsp90); Electron Paramagnetic Resonance (EPR); Oxidized Phospholipids; Radical
Authors: Sylvia Welker; Birgit Rudolph; Elke Frenzel; Franz Hagn; Gerhard Liebisch; Gerd Schmitz; Johannes Scheuring; Andreas Kerth; Alfred Blume; Sevil Weinkauf; Martin Haslbeck; Horst Kessler; Johannes Buchner Journal: Mol Cell Date: 2010-08-27 Impact factor: 17.970
Authors: Jan Kovár; Hana Stýbrová; Petr Novák; Marie Ehrlichová; Jaroslav Truksa; Michal Koc; Karin Kriegerbecková; Barbara Scheiber-Mojdehkar; Hans Goldenberg Journal: Cell Physiol Biochem Date: 2004