scholarly journals Subcellular localization of carboxylesterase‐4 in rat liver cells and its role as neutral cholesteryl ester hydrolase

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Snigdha Ghosh ◽  
Sajesh Parathath ◽  
Edward A Fisher ◽  
Earl H Harrison
1992 ◽  
Vol 70 (9) ◽  
pp. 800-803 ◽  
Author(s):  
Shobha Ghosh ◽  
W. McLean Grogan

Rabbit polyclonal antibodies were raised against rat liver bile salt-independent neutral cholesteryl ester hydrolase (CEH) and used for subcellular localization and immunological comparison with isoforms from other tissues. Antibodies exhibited a high degree of specificity for the liver CEH through all stages of purification and neutralized 70–80% of the activity of liver cytosolic CEH. They exhibited various levels of cross-reactivity with cytosolic proteins from other tissues, but reacted weakly with pancreatic and intestinal proteins and did not inhibit pancreatic CEH. Cytosol contained 78% of total cellular CEH activity and 75% of CEH immunoreactive protein. Washed microsomes contained 3% of CEH activity and 5% of CEH protein.Key words: cholesteryl esterase, polyclonal antibodies, rat liver, subcellular distribution.


1981 ◽  
Vol 193 (3) ◽  
pp. 743-748 ◽  
Author(s):  
S Frederiksen ◽  
H Flodgard ◽  
P Hellung-Larsen

The subcellular localization of the four major low-molecular-weight RNA components, D, C, A and L, was studied in rat liver cells. The cells were fractionated by a non-aqueous technique into a nuclear and a cytoplasmic fraction. The cytoplasm contained 43% of component D, 57% of component C and more than 80% of component L.


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