The kinetics and specificity of the interaction of nascent HepG2 LDL with the HepG2 LDL receptor were examined. 125I-Labeled HepG2 LDL and plasma LDL were bound by HepG2 cells in a specific and saturable manner at 4 degrees C. Competition studies with HepG2 LDL and plasma LDL indicated that both ligands bound to the same receptor. Scatchard analyses of the specific 4 degrees C-binding data revealed a Kd of 75 nM for HepG2 LDL and a Kd of 30 nM for plasma LDL suggesting that HepG2 LDL bind less efficiently to the HepG2 LDL receptor than plasma LDL. Binding, internalization and degradation studies carried out at 37 degrees C indicated that HepG2 cells are capable of catabolizing their own nascent LDL; however, under normal experimental conditions re-uptake of nascent LDL is quantitatively insignificant.