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Journal of Lipid Research, Vol 37, 1481-1487, Copyright © 1996 by Lipid Research, Inc.
T Tsujita, Y Matsuura and H Okuda
The basic protein protamine strongly inhibited hydrolysis of triolein
emulsified with soybean phosphatidylcholine (PC) by pancreatic and
carboxylester lipases; 10 micrograms/ml protamine, about 1000 times lower
than the concentration of bovine serum albumin for the same effect,
inhibited triolein hydrolysis completely. This inhibition was not affected
by the incubation pH or bile salt concentration. Two other basic proteins,
histone and purothionin, also inhibited hydrolysis of triolein emulsified
with soybean PC, but they did not inhibit triolein hydrolysis by gastric
lipase. When gum arabic was used as an emulsifier instead of soybean PC,
these basic proteins did not affect triolein hydrolysis by pancreatic or
carboxylester lipases. The effects of protamine on triolein hydrolysis by
pancreatic and carboxylester lipases was studied using various
phospholipids as emulsifiers. Protamine (10 micrograms/ml) did not inhibit
hydrolysis of triolein emulsified with dicaproyl PC (DCPC), phosphatidic
acid (PA), or phosphatidylserine (PS) by pancreatic and carboxylester
lipases. Conversely, protamine at high concentrations slightly stimulated
hydrolysis of triolein emulsified with DCPC or PA. Hydrolysis of
triolein-phosphatidylethanolamine (PE) emulsion was inhibited slightly by
protamine. The profiles of protamine inhibition of triolein-
phosphatidyl-N,N-dimethyl ethanolamine (PDME) and triolein-phosphatidyl-
N-monomethyl ethanolamine (PMME) emulsions were intermediate between those
of PC and PE emulsions. These results suggest that the phospholipid
species, especially choline moieties and fatty acid chain length, affect
the lipase inhibitory activity of protamine profoundly. In vivo, oral
administration of protamine to rats reduced and delayed the peak plasma
triacylglycerol concentration, but neither bovine serum albumin nor an
amino acid mixture with an amino acid composition identical to protamine
affected plasma triacylglycerol levels.
ARTICLES
Studies on the inhibition of pancreatic and carboxylester lipases by protamine
Department of Medical Biochemistry, School of Medicine, Ehime University, Japan.
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