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Title

THERMODYNAMIC DENATURATION OF HUMAN HEMOGLOBIN A IN AQUEOUS SODIUM N-DODECYL SULPHATE AS A FUNCTION OF PH

Pages

  109-115

Keywords

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Abstract

 In this paper, thermodynamic denaturation of human hemoglobin A derivatives (oxyhemoglobin and methemoglobin) in aqueous sodium n-dodecyl sulphate as a function of pH has been studied. The thermodynamic analysis reveals that maximum stability, DGD(H2o),and minimum stability, DG D(hc), of hemoglobin A derivatives in aqueous sodium n-dodecyl sulphate is both pH and temperature dependent. Variation of activation parameters (DGD, DGD and DSD) in the transition region depends on the presence of salt bridge, hydrogen bonding, van der Waal forces, changes in solvation and polarity at the reactive centers, as well as conformational mobility of hemoglobin A and sodium n-dodecyl sulphate within the active sites. The thermodynamic denaturation of hemoglobin A derivatives in aqueous anionic surfactant is independent of the spin state of the protein.

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    APA: Copy

    ABOLUWOYE, C.O., GADZEKPO, V.P.Y., NSIAH, F., & OKAI SAML, F.. (2002). THERMODYNAMIC DENATURATION OF HUMAN HEMOGLOBIN A IN AQUEOUS SODIUM N-DODECYL SULPHATE AS A FUNCTION OF PH. SCIENTIA IRANICA, 9(2), 109-115. SID. https://sid.ir/paper/289427/en

    Vancouver: Copy

    ABOLUWOYE C.O., GADZEKPO V.P.Y., NSIAH F., OKAI SAML F.. THERMODYNAMIC DENATURATION OF HUMAN HEMOGLOBIN A IN AQUEOUS SODIUM N-DODECYL SULPHATE AS A FUNCTION OF PH. SCIENTIA IRANICA[Internet]. 2002;9(2):109-115. Available from: https://sid.ir/paper/289427/en

    IEEE: Copy

    C.O. ABOLUWOYE, V.P.Y. GADZEKPO, F. NSIAH, and F. OKAI SAML, “THERMODYNAMIC DENATURATION OF HUMAN HEMOGLOBIN A IN AQUEOUS SODIUM N-DODECYL SULPHATE AS A FUNCTION OF PH,” SCIENTIA IRANICA, vol. 9, no. 2, pp. 109–115, 2002, [Online]. Available: https://sid.ir/paper/289427/en

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