کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2051433 1074200 2005 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Thermodynamics of phosphorylcholine and lysophosphatidylcholine binding to the major protein of bovine seminal plasma, PDC-109
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Thermodynamics of phosphorylcholine and lysophosphatidylcholine binding to the major protein of bovine seminal plasma, PDC-109
چکیده انگلیسی

PDC-109 binds to sperm plasma membranes by specific interaction with choline phospholipids and induces cholesterol efflux, a necessary event before capacitation – and subsequent fertilization – can occur. The binding of phosphorylcholine (PrC) and lysophosphatidylcholine (Lyso-PC) with PDC-109 was investigated by monitoring the ligand-induced changes in the absorption spectrum of PDC-109. At 20 °C, the association constants (Ka), for PrC and Lyso-PC were obtained as 81.4 M−1 and 2.02 × 104 M−1, respectively, indicating that the binding of Lyso-PC to PDC-109 is 250-fold stronger than that of PrC. From the temperature dependence of the Ka values, enthalpy of binding (ΔH0) and entropy of binding (ΔS0), were obtained as −79.7 and −237.1 J mol−1 K−1 for PrC and −73.0 kJ mol−1 and −167.3 J mol−1 K−1 for Lyso-PC, respectively. These results demonstrate that although the binding of these two ligands is driven by enthalpic forces, smaller negative entropy of binding associated with Lyso-PC results in its significantly stronger binding.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 579, Issue 13, 23 May 2005, Pages 2933–2938
نویسندگان
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