caa a22 4500 465766390 CHVBK 20180323111915.0 cr unu---uuuuu 170327e19900401xx s 000 0 eng 10.1007/BF02535751 doi (NATIONALLICENCE)springer-10.1007/BF02535751 Separation and differential activation of rat liver cytosolic cholesteryl ester hydrolase, triglyceride lipase and retinyl palmitate hydrolase by cholestyramine and protein kinases [Elektronische Daten] [Shobha Ghosh, Maria Kounnas, W. Grogan] Cholesteryl ester hydrolase (CEH), triacylglycerol lipase (TGL) and retinyl palmitate hydrolase (RPH) were measured in 104,000 ×g supernatants from rat liver under optimal conditions for measurement of cytosolic CEH. Similar levels of hydrolytic activity were seen with oil droplet dispersions of cholesteryl oleate, trioleoylglycerol and retinyl palmitate. No cytosolic TGL activity was seen with substrate presented in the triton-albumin emulsion used for measurement of lipoprotein lipase-like TGL associated with hepatic plasma membrane. Cytosolic CEH, TGL and RPH were differentially partially purified by both ammonium sulfate precipitation and anion exchange fast protein liquid chromatography (FPLC). Of the three activities, only CEH was stimulated by cholestyramine feeding and by activators of protein kinases A and C. All three activities were inhibited by alkaline phosphatase treatment, although to different degrees. It is concluded that these activities are catalyzed by at least three differentially regulated enzymes with a high degree of specificity for their respective substrates. American Oil Chemists' Society, 1990 Ghosh Shobha Department of Biochemistry and Molecular Biophysics, Medical College of Virginia, Virginia Commonwealth University, 23298-0614, Richmond, VA aut Kounnas Maria Department of Biochemistry and Molecular Biophysics, Medical College of Virginia, Virginia Commonwealth University, 23298-0614, Richmond, VA aut Grogan W. Department of Biochemistry and Molecular Biophysics, Medical College of Virginia, Virginia Commonwealth University, 23298-0614, Richmond, VA aut Lipids Springer-Verlag 25/4(1990-04-01), 221-225 0024-4201 25:4<221 1990 25 11745 https://doi.org/10.1007/BF02535751 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF02535751 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ghosh Shobha Department of Biochemistry and Molecular Biophysics, Medical College of Virginia, Virginia Commonwealth University, 23298-0614, Richmond, VA aut NATIONALLICENCE 700 1- Kounnas Maria Department of Biochemistry and Molecular Biophysics, Medical College of Virginia, Virginia Commonwealth University, 23298-0614, Richmond, VA aut NATIONALLICENCE 700 1- Grogan W. Department of Biochemistry and Molecular Biophysics, Medical College of Virginia, Virginia Commonwealth University, 23298-0614, Richmond, VA aut NATIONALLICENCE 773 0- Lipids Springer-Verlag 25/4(1990-04-01), 221-225 0024-4201 25:4<221 1990 25 11745 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer