Purification and characterization of cholesterol esterase from porcine pancreas.

[1]  H. Brockman,et al.  Effects of colipase and taurodeoxycholate on the catalytic and physical properties of pancreatic lipase B at an oil water interface. , 1976, The Journal of biological chemistry.

[2]  L. Gallo,et al.  Purification and properties of subunits of sterol ester hydrolase from rat pancreas. , 1975, Archives of biochemistry and biophysics.

[3]  C. R. Treadwell,et al.  Pancreatic juice cholesterol esterase. Studies on molecular weight and bile salt-induced polymerization. , 1972, Archives of biochemistry and biophysics.

[4]  J. Teale,et al.  High and low molecular weight forms of pancreatic cholesterol esterase. , 1972, Biochemical and biophysical research communications.

[5]  L. Sarda,et al.  Purification from porcine pancreas of two molecular species with lipase activity. , 1969, Biochimica et biophysica acta.

[6]  K. Weber,et al.  The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. , 1969, The Journal of biological chemistry.

[7]  H. Kothari,et al.  Purification and properties of pancreatic juice cholesterol esterase. , 1969, The Journal of biological chemistry.

[8]  M. L. Bender,et al.  The kinetics of the alpha-chymotrypsin-catalyzed hydrolysis of p-nitrophenyl acetate. , 1962, Biochemistry.

[9]  J. Ganguly,et al.  Studies on cholesterol esterases of the small intestine and pancreas of rats. , 1962, The Biochemical journal.

[10]  Chaikoff Il,et al.  Purification and properties of pancreatic cholesterol esterase. , 1957 .

[11]  C. Erlanson Purification, properties, and substrate specificity of a carboxylesterase in pancreatic juice. , 1975, Scandinavian journal of gastroenterology.

[12]  C. Erlanson p-nitrophenylacetate as a substrate for a carboxyl-ester hydrolase in pancreatic juice and intestinal content. , 1970, Scandinavian journal of gastroenterology.