Hepatic clearance of rat liver aspartate aminotransferase isozymes: Evidence for endocytotic uptake via different binding sites on sinusoidal liver cells
Seikoh Horiuchi, Yukio Kamimoto, Yoshimasa Morino – 1 May 1985 – Rat liver aspartate aminotransferase (AAT) (EC 2.6.1.1) exists in two isozymic forms, cytosolic (c‐AAT) and mitochondrial (m‐AAT). The previous study (Kamimoto, Y. et al., Hepatology an accompanying paper in this issue) demonstrated that these isozymes were cleared from blood at different half‐lives via adsorptive endocytosis by sinusoidal liver cells. To understand the cellular mechanism for the differential uptake of the isozymes, we have further studied in vivo uptake of 125I‐labeled AAT isozymes by sinusoidal cells.