Fractionation, biochemical characterization and lysosomal phospholipases of human liver

FEBS Letters

Löffler, Bernd-Michael¹  Kunze, Hans¹ 

[1] Max-Planck-Institut für Experimentelle Medizin, Hermann-Rein-Straße 3, D-3400 Göttingen, FRG

关键词: Subcellular fractionation;    Marker enzyme;    Phospholipase;    Chloroquine;    Mepacrine;    Primaquine;    (Human liver;    Rat liver);   

DOI  :  10.1016/0014-5793(87)80755-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Human liver was homogenised and fractionated by differential centrifugation, and the subcellular fractions were characterised biochemically. Absolute values and distribution patterns of protein and marker enzyme activities obtained from human liver have also been compared with those from rat liver. In addition, acid phospholipase activities have been studied in human liver. On the basis of product formation from stereo-specifically radiolabeled phosphatidylethanolamine substrates, lysosomal phospholipases A₁ and A₂ with optimal activities at pH 4.7 have been identified in human liver. Acid phospholipase C and lysophospholipase activities, however, were not found in human liver. Cationic amphiphilic drugs inhibited the activities of the acid phospholipases A in human and rat liver lysosomes to about the same extent.

【 授权许可】

Unknown