scholarly journals Characterization of multiple forms of cholesteryl ester hydrolase in the rat testis.

1984 ◽  
Vol 259 (12) ◽  
pp. 7433-7438 ◽  
Author(s):  
L A Durham ◽  
W M Grogan
Lipids ◽  
1984 ◽  
Vol 19 (10) ◽  
pp. 714-720 ◽  
Author(s):  
Mitsuo Tanaka ◽  
Ryooji Yonekura ◽  
Toshihiro Iio ◽  
Toshikazu Tabata

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.


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