Abstract:
:The rate of hydrolysis of long chain triglycerides by pure bovine pancreatic lipase has been determined in the presence of variable amounts of bile salts and colipase. Cofactor-free lipase is strongly inhibited by sodium taurodesoxycholate and by mixed bovine bile salts at concentrations higher than the critical micellar concentration. Bile salt inhibited lipase is reactivated by the addition of bovine colipase. Gel filtration of pancreatic juice from several species (Cow, dog, pig) on Sephadex G 100 allows the separation of lipase from colipase. It is found that the enzyme catalyzed hydrolysis of long chain triglycerides by pancreatic lipase from one species is activated by the addition of colipase from other species. Studies on the activation of pancreatic lipase by colipase in the presence of bile salts allowed the re-evaluation of optimal conditions for the determination of lipase and the development of a procedure to assay colipase.
journal_name
Biochimiejournal_title
Biochimieauthors
Rathelot J,Julien R,Canioni P,Coeroli C,Sarda Ldoi
10.1016/s0300-9084(76)80572-xkeywords:
subject
Has Abstractpub_date
1975-01-01 00:00:00pages
1117-22issue
10eissn
0300-9084issn
1638-6183pii
S0300-9084(76)80572-Xjournal_volume
57pub_type
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