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Information Journal Paper

Title

DENATURATION BEHAVIOR OF FREE AND CA+2 BOUND MRP8/MRP14 PROTEIN

Pages

  211-219

Keywords

FREE AND CA+2 BOUND MRP8/MRP14; SDS; UREA 

Abstract

 The denaturation behavior of free and calcium saturated MRP8/MRP14 (calprotectin) in sodium dodecyl sulphate (SDS) and urea was studied by fluorescence spectroscopy. The sigmoidal denaturation curve was plotted in order to estimate the thermodynamic parameters, assuming a two-state mechanism in terms of the Pace model. SDS, anionic surfactant, affects free and calcium saturated MRP8/MRP14 at a millimolar level as a result of direct interaction between free and calcium saturated protein and surfactant as an amphipatic molecule. Urea also affects free and calcium saturated MRP8/MRP14 but at a molar level and as a result of indirect interaction with the surrounding of free and calcium saturated protein (a change in the water structure). The thermodynamic data indicate that ΔG°H2O of saturated human MRP8/MRP14 is larger than that of free form. Therefore, calcium bound protein is more stable and resistant to the denaturant agent.

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  • Cite

    APA: Copy

    GHAVAMI, S., KARAMI TEHRANI, FATEMEH, HASHEMI, M., & FARZAMI, B.. (2003). DENATURATION BEHAVIOR OF FREE AND CA+2 BOUND MRP8/MRP14 PROTEIN. JOURNAL OF SCIENCES ISLAMIC REPUBLIC OF IRAN, 14(3), 211-219. SID. https://sid.ir/paper/531720/en

    Vancouver: Copy

    GHAVAMI S., KARAMI TEHRANI FATEMEH, HASHEMI M., FARZAMI B.. DENATURATION BEHAVIOR OF FREE AND CA+2 BOUND MRP8/MRP14 PROTEIN. JOURNAL OF SCIENCES ISLAMIC REPUBLIC OF IRAN[Internet]. 2003;14(3):211-219. Available from: https://sid.ir/paper/531720/en

    IEEE: Copy

    S. GHAVAMI, FATEMEH KARAMI TEHRANI, M. HASHEMI, and B. FARZAMI, “DENATURATION BEHAVIOR OF FREE AND CA+2 BOUND MRP8/MRP14 PROTEIN,” JOURNAL OF SCIENCES ISLAMIC REPUBLIC OF IRAN, vol. 14, no. 3, pp. 211–219, 2003, [Online]. Available: https://sid.ir/paper/531720/en

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