Cytof lowmetric Analysis of Binding Pattern and A New Binding Kinetic Constant for an Enterovirus and Receptor

Abstract

A bovine enterovirus (MZ-468) was adsorbed to Sarcoma-180 cells at 4°C. The cells were reacted with FITC-labeled IgG antibody for the virus and were studied with a laser fluorescence cytoflowmeter. From the histograms, binding-saturation of receptors was observed and the dissociation constant (Kd) was estimated. A new binding rate constant was deduced from the change of the ratio of virus-adsorbed cells against time and virus concentration. The constant has a dimensions of (cm³/min·receptor-site) and probably represents the receptor class on a cell with the highest rate constant.