Biophysical investigations on the interaction of the major bovine seminal plasma protein, PDC-109, with heparin.

PDC-109, the major bovine seminal plasma protein, binds to sperm plasma membrane and modulates capacitation in the presence of heparin. In view of this, the PDC-109/heparin interaction has been investigated employing various biophysical approaches. Isothermal titration calorimetric studies yielded the association constant and changes in enthalpy and entropy for the interaction at 25 °C (pH 7.4) as 1.92 (±0.2) × 105 M–1, 18.6 (±1.6) kcal M–1, and 86.5 (±5.1) cal M–1 K–1, respectively, whereas differential scanning calorimetric studies indicated that heparin binding results in a significant increase in the thermal stability of PDC-109. The affinity decreases with increase in pH and ionic strength, consistent with the involvement of electrostatic forces in this interaction. Circular dichroism spectroscopic studies indicated that PDC-109 retains its conformational features even up to 70–75 °C in the presence of heparin, whereas the native protein unfolds at about 55 °C. Atomic force microscopic studies demons...