Motif 2 in adenosine kinase homologous ginseng polypeptide showed affinity to D-ribose by capillary zone electrophoresis and surface plasmon resonance.

Affinity capillary electrophoresis (ACE) and surface plasmon resonance (SPR) were applied to the analysis of anti-lipolytic acidic tetradecapeptide from Panax ginseng roots. The ginseng polypeptide (GPP) and modified GPPs were chemically synthesized and their affinity to D-ribose and adenosine was examined by ACE and SPR. GPP had affinity to D-ribose and adenosine and the binding constants (Kb) to GPP were calculated by both methods (Kb = 1.04 x 10(4) mol-1 to D-ribose by ACE and Kb = 1.91 x 10(4) mol-1 to adenosine by SPR). Most of the modified GPPs lost their affinity to D-ribose and adenosine through substitution or rearrangement of the amino acids.