Flow cytometry and biochemical analysis of DNA degradation characteristic of two types of cell death

Interactions of tuftsin (Thr-Lys-Pro-Arg) with bovine serum albumin (BSA) were analysed by fluorescence spectroscopy and circular dichroism. The data show that tuftsin interacts weakly with BSA, but this interaction is considerably enhanced by introducing an apolar substituent at the C-terminus of the tetrapeptide. It is suggested that strong binding of tuftsin to albumin in blood may enhance its macrophage-stimulating activity in vivo.