Identification of a non-specific carboxylesterase in human pancreas using vinyl 8-phenyloctanoate as a substrate.
Human pancreatic tissue, pancreatic juice and sera of patients suffering from acute pancreatitis contain a vinyl 8-phenyloctanoate hydrolysing activity which was separated from true pancreatic lipase (EC 3.1.1.3). The enzyme, preliminary called "non-specific pancreatic carboxylesterase, was partially purified from human pancreatic tissue by DEAE-cellulose chromatography. Its molecular weight was found to be 54 000 by gel filtration on Sephadex G-100. The isoelectric point was estimated as 4.65 by isoelectric focusing. The results explain the poor correlation obtained when determinations of "serum lipase activity" using triolein and vinyl 8-phenyloctanoate as substrates are compared. However, since non-specific pancreatic carboxylesterase is liberated into the serum, determination of this new enzyme provides additional information in the diagnosis of pancreatic diseases.
D002210:Caprylates / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000032:analysis* / Q000097:blood; D006801:Humans; D008049:Lipase / Q000032:analysis; D010179:Pancreas / Q000201:enzymology*; D010189:Pancreatic Juice / Q000201:enzymology; D010195:Pancreatitis / Q000201:enzymology; D014753:Vinyl Compounds / Q000378:metabolism
D002210:Caprylates; D014753:Vinyl Compounds; C020545:vinyl 8-phenyloctanoate; D002265:Carboxylic Ester Hydrolases; D008049:Lipase