エンドトキシン投与時におけるラット肝病変の研究　(I) 分離した肝実質細胞および非実質細胞におけるリソソーム酵素活性と酸性ホスファターゼのアイソザイムパターン

概要

論文の詳細を見る
Lysosomal enzyme activities and isozyme patterns of acid phosphatase were studied in parenchymal cells (PC) and non-parenchymal cells (NPC) isolated separately from normal rat livers. The NPC suspensions prepared by pronase treatment were composed of heterogeneous cell types. About 50-60% of NPC were Kupffer cells and about 30% of NPC were endothelial cells. The activities of acid phosphatase using adenosine monophosphate (AMP), cytidine monophosphate (CMP), phenyl phosphate (PhP) and β-glycerophosphate (bGP) as substrates and the β-glucuronidase activity were compared between homogenates of PC and NPC. When AMP or CMP was used as a substrate, the specific activity of acid phosphatase per protein in PC was found to be higher than those in NPC. On the other hand, the activity with PhP and the /3-glucuronidase activity were higher in NPC than in PC. The acid phosphatase activity with bGP was about the same in both cell homogenates. The isozyme patterns of acid phosphatase were examined by electrophoresis on the cellulose acetate membrane. Among three major isozyme bands of acid phosphatase in adult rat liver, the most anodic band was the dominant isozyme of NPC and the other two bands were of PC.These results indicate that acid phosphatase in rat liver is qualitatively and quantitatively different between PC and other cell types.
札幌医科大学の論文
1978-08-01