Experimental results are presented for the separation of monoclonal IgM antibodies from hybridoma cell cultures using tangential flow ultrafiltration with total recycle of the retentate. IgM antibodies are pentameric immunoglobulin molecules with a molar mass of 900 kDa and a tip-to-tip distance of 38 nm. The major impurity (foulant) in the supernatant sample was albumin, whose molar mass and diameter are 67 kDa and 7 nm, respectively. The antibody (product) recovery rate, variations in the permeation velocity and the time for a 90%-reduction in feed volume were investigated using 100 and 300 kDa NMWCO membranes at three transmembrane pressures and two tangential velocities. A model is also presented, in which the ultrafiltration process is divided into two regimes : the surface fouling regime (characterized by the adsorption of antibody molecules on the membrane surface) and the internal fouling regime (characterized by pore-blockage due to deposition of foulant protein molecules). Approximately 16% of the effective membrane area was blocked in the surface fouling regime. The model predictions are in satisfactory agreement with the experimental results.