In this study, the biochemical characteristics of proteolipids of rat liver and kidney homogenates were compared. In all preparations, the proteo‐lipids were eluted at the void volume of the Biogel A‐15 m column after gel chromatography, and a molecular weight over 15×106 was estimated. Electron microscopy of the concentrated void volume fractions showed globular particles with diameters of 30–100 nm for liver (LSP) and 30–60 nm for kidney (KSP) preparations that might be formed from plasma membrane fragments. After ultracentrifugation in a CsCl gradient, rat LSP and KSP floated in a small density range from 1.16–1.17 g/ml. There was no significant difference between the relative percentages of phospholipids, triglycerides and cholesterol of both proteo‐lipids. However, the relative mean amount of total protein in rat KSP (60.4% vs 50.4%) was significantly higher and the content of free fatty acids (4.3% vs 12.6%) significantly lower compared to rat LSP. SDS‐PAGE revealed at least 12 protein subunits ranging from 15,000–130,000 in both preparations, but one protein of about Mr 49,000 might represent a liver specific component. The isolated proteo‐lipids from rat liver and kidney homogenates showed similar biochemical characteristics as those from human sources, which could explain the known cross‐reactivity of antibodies against these preparations.The putative function of these proteo‐lipids is not known, although there is some evidence from human studies that they carry receptor proteins.