Unfolding and release of heme from human hemoglobins A,S and F |
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| Institution: | 1. College of Longrun Pu-erh Tea, Yunnan Agricultural University, Kunming, Yunnan 650201, China;2. State Key Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University, Hefei, 230036 Anhui, China;3. National Key Facility for Crop Gene Resources and Genetic Improvement, Institute of Crop Sciences, Chinese Academy of Agricultural Sciences, Beijing 100081, China;4. State Key Laboratory of Conservation and Utilization of Bio-resources in Yunnan, Yunnan Agricultural University, Kunming, Yunnan 650201, China;5. The Key Laboratory of Medicinal Plant Biology of Yunnan Province, National & Local Joint Engineering Research Center on Germplasm Innovation & Utilization of Chinese Medicinal Materials in Southwestern China, Yunnan Agricultural University, Kunming, Yunnan 650201, China;6. Hangzhou Tea Research Institute, CHINA COOP, Hangzhou 310016, China;1. School of Chemistry and Chemical Engineering, Liaocheng University, Liaocheng University, Liaocheng, Shandong 252059, PR China;2. School of Life Science, Liaocheng University, Liaocheng University, Liaocheng, Shandong 252059, PR China;1. Dipartimento di Scienze dell’Ambiente, della Sicurezza, del Territorio, degli Alimenti e della Salute, Università di Messina, Viale F. Stagno d’Alcontres 31, 98166 Messina, Italy;2. Dipartimento di Fisica e Scienze della Terra, Università di Messina, Viale F. Stagno D’Alcontres 31, 98166 Messina, Italy;3. CNR-IPCF, Istituto per i Processi Chimico-Fisici, Viale F. Stagno D’Alcontres 33, 98158 Messina, Italy |
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| Abstract: | - 1.1. Analysis of the Soret spectra of hemoglobins A, S and F has been used to determine the extent of heme exposure and release from these hemoglobins in the presence of several solvent perturbants.
- 2.2. Oxyhemoglobin S unfolding in the presence of either urea or propyl urea resulted in greater heme exposure and release than either oxyhemoglobins A or F.
- 3.3. Methemoglobin formation resulted in lower denaturation midpoints for each hemoglobin compared to the reduced oxyhemoglobin state; methemoglobin F had the lowest denaturation midpoint under isothermal denaturing conditions.
- 4.4. Rate of heme exposure was greater for oxyhemoglobin S than oxyhemoglobin A in the presence of 200 μM the anionic detergent sodium dodecyl sulfate.
- 5.5. Evidence for increased levels of heme release in hemoglobin S may be related to the greater tendency of sickled red cell membranes to undergo lipid oxidation.
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