Purification and characterization of cholesterol esterase from porcine pancreas.
暂无分享,去创建一个
[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.