Purification and characterization of a carboxyl ester hydrolase from human pancreatic juice

Biochim Biophys Acta. 1978 Nov 10;527(1):142-9. doi: 10.1016/0005-2744(78)90263-2.


A carboxyl ester hydrolase has been purified 20-fold from human pancreatic juice. It is a glycoprotein with a molecular weight of 100 000. It contains 9% neutral and amino carbohydrates and the amino acid composition is characterized by a high content of proline residue (12.7%). The enzyme catalyzes the hydrolysis of p-nitrophenylacetate and the activity increases in the presence of biliary salts; V is not modified but Km is decreased 10 times by addition of biliary salts. The enzyme migrates on Sephadex G-200 as a protein with a molecular weight of 300 000. This behaviour does not seem to be due to a polymerization but to a peculiar configuration of the enzyme.

MeSH terms

  • Amino Acids / analysis
  • Carbohydrates / analysis
  • Carboxylic Ester Hydrolases / isolation & purification
  • Carboxylic Ester Hydrolases / metabolism*
  • Humans
  • Kinetics
  • Molecular Weight
  • Pancreatic Juice / enzymology*


  • Amino Acids
  • Carbohydrates
  • Carboxylic Ester Hydrolases