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Inhibition of Human Hemoglobin Autoxidaiton by Sodium n-Dodecyl Sulphate
Reza, Dayer Mohammad,Ali Akbar, Moosavi-Movahedi,Parviz, Norouzi,Ghourchian, Ghourchian,Hedayat-Olah, Hedayat-Olah,Shahrokh, Safarian 생화학분자생물학회 2002 Journal of biochemistry and molecular biology Vol.35 No.4
The effect of sodium n-dodecyl sulphate (SDS) on hemoglobin autoxidation was studied in the presence of a 100mM phosphate buffer (pH 7.0) by different methods. These included spectorphotometry, fluorescence technique, cyclic voltametry, differential scanning calorimetry, and densitometry. Spectroscopic studies showed that SDS concentrations up to 1 mM increased deoxy-, decreases oxy-, and had no significant effect on the met- conformation of hemoglobin. Therefore, a SDS concentration up to 1 mM increased the deoxy form of hemoglobin as the folded, compact state and decreases the oxy conformation. The turbidity measurements and differential scanning calorimetry techniques indicated a more stable conformation for hemoglobin in the presence of SDS up to 1mM. Electrochemical studies also confirmed a more difficult oxidation under these conditions. The induction of the deoxy form in the presence of SDS was confirmed by densitometry techniques. The compact structure of deoxyhemoglobin blocks the formation of met-conformation in low SDS concentrations.
Inhibition of Human Hemoglobin Autoxidation by Sodium n - Dodecyl Sulphate
(Dayer Mohammad Reza),(Moosavi Movahedi Ali Akbar),(Norouzi Parviz),(Ghourchian),(Hedayat Olah),(Safarian Shahrokh) 생화학분자생물학회 2002 BMB Reports Vol.35 No.4
The effect of sodium n-dodecyl sulphate (SDS) on hemoglobin autoxidation was studied in the presence of a 100 mM phosphate buffer (pH 7.0) by different methods. These included spectrophotometry, fluorescence technique, cyclic voltametry, differential scanning calorimetry, and densitometry. Spectroscopic studies showed that SDS concentrations up to 1 mM increased deoxy-, decreases oxy-, and had no significant effect on the met- conformation of hemoglobin. Therefore, a SDS concentration up to 1 mM increased the deoxy form of hemoglobin as the folded, compact state and decreases the oxy conformation. The turbidity measurements and differential scanning calorimetry techniques indicated a more stable conformation for hemoglobin in the presence of SDS up to 1 mM. Electrochemical studies also confirmed a more difficult oxidation under these conditions. The induction of the deoxy form in the presence of SDS was confirmed by densitometry techniques. The compact structure of deoxyhemoglobin blocks the formation of met-conformation in low SDS concentrations.