Purification from porcine pancreas of two molecular species with lipase activity

Verger, Robert; Haas, G.H. de; Sarda, Louis; Desnuelle, P.

doi:10.1016/0005-2795(69)90075-0

Cited by 230 publications

(71 citation statements)

References 22 publications

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“…In many cases their bile salt concentrations are low (18), but they digest the milk lipids rather efficiently (19 (21). Lipase and colipase were purified from pig pancreas according to Verger et al (22) and Erlanson and Borgstrom (23). In the purification of lipase, the CM-cellulose step, which separates two forms of the lipase (A and B), was omitted.…”

Section: Introductionmentioning

confidence: 99%

Colipase enhances hydrolysis of dietary triglycerides in the absence of bile salts.

Bläckberg¹,

Hernell²,

Bengtsson³

et al. 1979

J. Clin. Invest.

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Section: Introductionmentioning

confidence: 99%

Colipase enhances hydrolysis of dietary triglycerides in the absence of bile salts.

Bläckberg¹,

Hernell²,

Bengtsson³

et al. 1979

J. Clin. Invest.

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“…Some lipases are shown to exist in multiple form in animal tissues such as rat liver,l) rat adipose tissue,2) porcine pancreas 3 ) and human adipose tissue,4) and in some species of mold. 5 • 6 ) With respect to the plant lipase, the existence of two lipases, acid and alkaline lipase, has been pointed out in castor bean endosperm.…”

mentioning

confidence: 99%

Purification and Characterization, of Rice Bran Lipase II

Aizono

Funatsu

Fujiki

et al. 1976

Agricultural and Biological Chemistry

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“…Sodium deoxycholate was obtained from Merck, Darmstadt, Germany and gum arabic was from Sigma Chemical Co., St. Louis, Mo., USA. Bile salt-stimulated lipase was purified from human milk as previously described (3) and porcine pancreatic lipase, purified as described (36), was a generous gift from Dr. R. Verger, Marseille, France. The specific activities were 50 and 300 pmole fatty acid released per min and mg protein (trioleylglycerol/gum arabic emulsion, pH 6.5) for the respective lipase.…”

Section: Methodsmentioning

confidence: 99%

Digestion of Human Milk Lipids: Physiologic Significance of sn-2 Monoacylglycerol Hydrolysis by Bile Salt-Stimulated Lipase

Hernell

Bläckberg

1982

Pediatr Res

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SummaryThe bile salt-stimulated lipase secreted with human milk was found to be devoid of positional specificity, i.e., it hydrolyzed emulsified triacylglycerols to glycerol and fatty acids. It also hydrolyzed micellar sn-2 monoacylglycerols. This is in contrast to pancreatic lipase which has a pronounced preferrance for hydrolysis of sn-1 and sn-3 ester bonds. When the two enzymes were operating together, as in the intestine of the infant fed raw human milk, the sn-2 monoacylglycerols formed by pancreatic lipase served as an excellent substrate for bile salt-stimulated lipase. Thus, the end products of triacylglycerol hydrolysis became glycerol and fatty acids and not sn-2 monoacylglycerol and fatty acids. The bile salt-stimulated lipase also catalyzed incorporation of fatty acids into acylglycerols to a much lesser extent than did pancreatic lipase. Together these two effects of bile salt-stimulated lipase have a promoting effect on the overall process of intraluminal lipolysis.In newborn infants, with low intraduodenal bile salt concentrations, glycerol and fatty acids also should be more readily absorbed than monoacylglycerol and fatty acids. Thus, by serving as a complement to pancreatic lipase, bile salt-stimulated lipase can ensure efficient utilization of milk lipids also in infants with immature endogenous mechanisms for fat digestion and absorption.In the healthy human adult, digestion and absorption of dietary fat is almost complete, i.e., at least 95% of consumed fat is absorbed. The corresponding figures reported for newborn infants vary widely but, are especially for preterm infants often considerably lower (9,11,12,30,34,38). In these infants an impaired overall process of fat digestion and absorption has been attributed mainly to low intraduodenal concentrations of pancreatic lipase (15, 27, 39) and bile salts (8,26,35).Human milk contains a potent lipase, the bile salt-stimulated lipase, which supplement the low pancreatic lipase concentrations (16, for review see 18,19). This can explain why human milk fat is more efficiently utilized than fat from formulas based on cow's milk (12,23,37). Strong evidence that the bile salt-stimulated lipase has an important role in the digestion of milk lipids in the newborn comes from the recent observation that heat-treatment of human milk reduces fat absorption by approximately one third in preterm infants (1,38). Previous studies have established that this lipase contributes to hydrolysis of milk triacylglycerols and vitamin A esters (14,17). An additional, perhaps more important role of this lipase, might be to hydrolyze the monoacylglycerols generated by pancreatic lipase. Due to its positional specificity, pancreatic lipase hydrolyzes only two of the three ester bonds in a triacylglycerol molecule (7,24). Furthermore, this enzyme catalyzes not only hydrolysis but also esterification (4). Therefore, it soon reaches an equilibrium state where the rate of formation of di-and triacylglycerols by acylation of monoacylglycerols equals the rate of hydrolysis. F...

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Purification from porcine pancreas of two molecular species with lipase activity

Cited by 230 publications

References 22 publications

Colipase enhances hydrolysis of dietary triglycerides in the absence of bile salts.

Colipase enhances hydrolysis of dietary triglycerides in the absence of bile salts.

Purification and Characterization, of Rice Bran Lipase II

Digestion of Human Milk Lipids: Physiologic Significance of sn-2 Monoacylglycerol Hydrolysis by Bile Salt-Stimulated Lipase

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