99mTc-labelled polyclonal human immunoglobulin (HIG) has been shown to be able to localize inflammatory sites. Hypothetically these immunoglobulins bind directly to bacteria, HIG binds directly to Fc-receptors on the surface membrane of leucocytes or HIG simply passes vessels of increased permeability. To collect further information experiments were carried out in vitro with the blood of human volunteers. 0.5 mg 99mTc-HIG, 2 mg 99mTc-human albumin and 0.5 mg 99mTc-labelled murine monoclonal antigranulocyte antibodies were added to in vitro isolated human "mixed" leucocyte pellets and to 30 ml whole blood of 6 healthy volunteers. The whole blood and the directly labelled leucocyte pellet were layered and separated on a discontinuous Percoll/plasma gradient. The activity distribution was measured within the gradient. The 99mTc-HIG labelled gradients showed a significant uptake of the activity within the monocyte band whereas the 99mTc-albumin gradients showed no specific albumin uptake in any cellular band. The 99mTc-antibody labelled gradients showed a significantly increased uptake on granulocytes. It is concluded that in man a specific monocyte-associated uptake and binding mechanism of 99mTc-HIG plays an important role in the localisation of inflamed sites.