Fate of trypsin and chymotrypsin in the human small intestine.

Goldberg, David M.; Campbell, R.; Roy, A. D.

doi:10.1136/gut.10.6.477

Cited by 49 publications

(19 citation statements)

References 33 publications

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“…The assay of amylase, trypsin, and chymotrypsin was reasonably safe. Our observations are in line with the data of G oldberg et al [10] who noted that trypsin is hardly less stable in vitro than chymotrypsin in human ileal fluid. On the other hand, lipase was liable to rapid inactivation and it was manda tory to defrost the aliquots kept for lipase as late as possible before the assays.…”

Section: Assay Conditions and Stability O F Pancreatic Hydrolases In supporting

confidence: 83%

A Comparison of Enzyme Activities in Duodenal Aspirate Following Injection of Secretin, Caerulein, and Cholecystokinin

Vandermeers‐Piret¹,

Vandermeers²,

Rathé³

et al. 1974

Digestion

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A comparison has been made of the pattern of pancreatic enzyme activities in the duodenal juice of 32 healthy subjects, upon intravenous injection of GIH secretin (1 clinical unit/kg body weight), Farmitalia caerulein (40 ng/kg), or GIH cholecystokinin (1 Ivy dog u/kg), given alone or combined (according to 3 submaximum rapid injection schedules). Enzymatic activities were measured in 5- to 10-min duodenal aspirates. A close correlation between trypsin and chymotrypsin activities was evident under all circumstances. On the other hand there was an apparent delay in amylase and lipase responses after the bolus administration of caerulein or cholecystokinin.

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Section: Assay Conditions and Stability O F Pancreatic Hydrolases In supporting

confidence: 83%

A Comparison of Enzyme Activities in Duodenal Aspirate Following Injection of Secretin, Caerulein, and Cholecystokinin

Vandermeers‐Piret¹,

Vandermeers²,

Rathé³

et al. 1974

Digestion

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“…This is much later than the peak level of serum %-amino nitrogen, which occurs one It after a protein meal [8], During this time, much of the enzymes would become adsorbed to intestinal cells and debris [9,111 and reach the terminal ileum in an insoluble form. Indeed we have presented evidence suggesting that the greater part of the pancreatic output of trypsin and chym otrypsin passes into the colon [10], and it is hard to see why exogenous enzymes should not behave in a similar fashion.…”

Section: Discussionmentioning

confidence: 99%

“…The latter in turn is only about one-third of the total am ount of trypsin and one-eighth of the total am ount of chymotrvpsin recovered from patients on ileal drainage who were not given any oral enzymes [10,21]. It is difficult to envisage such a small increase effecting any alteration in blood or serum enzymes, the more so since it is a m atter of considerable doubt whether there is any pancreatic trypsin present in hum an serum.…”

Section: Discussionmentioning

confidence: 99%

“…We became interested in this question during work aimed at eluci dating the fate of pancreatic enzymes in the hum an intestine [10J and were further stim ulated by finding that trypsin and chym otryp sin became adsorbed to intestinal mucosal cells and intracellular organelles under physiological conditions [9,11]. A re-exam ination of the absorption of oral enzymes therefore seemed w arranted.…”

Section: Introd Actionmentioning

confidence: 99%

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On the Absorption of Pancreatic Enzymes from the Intestine in Man

Goldberg¹,

Campbell²,

Roy³

1970

Digestion

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Enteric-coated trypsin and chymotrypsin were given orally to 12 fasted human subjects in a dose of 200 mg and 100 mg respectively. Estimation of trypsin and chymotrypsin in blood and serum revealed no consistent change in activity over the succeeding 9 h with respect to the zero-time test value, or to the values for the corresponding time intervals on a separate occasion omitting oral enzymes. The trypsin-inhibitor activity of serum was likewise unaltered in 4 subjects in whom this determination was made. Trypsin and chymotrypsin, administered in a dose of 200 mg of each to four subjects by duodenal intubation also failed to alter the blood and serum levels of these enzymes. In addition to these results, further reasons are given for regarding intestinal absorption of pancreatic enzymes as currently unproven.

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“…We have given elsewhere our reasons for regarding this output as closely related to that of the pancreas (Roy et al, 1967;Goldberg, Campbell, and Roy, 1969) and consider the present findings indicative of a failure by Trasylol to diminish endogenous pancreatic enzyme secretion, in contrast to other workers who found a reduction in the output of enzymes when the gland was stimulated by exogenous pancreatic stimulants (Schultis and Rick, 1964). These results also throw doubt on the biological efficacy of the increased trypsin inhibitors in the pancreatic juice of patients given Trasylol (Morgan et al, 1968).…”

Section: Discussionmentioning

confidence: 99%

Failure of Trasylol to reduce intestinal content of trypsin and chymotrypsin in man

Goldberg¹,

Campbell²,

Roy³

1970

Gut

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SUMMARY The daily output of trypsin and chymotrypsin was measured in the stools of four patients with an established ileostomy under controlled dietary and metabolic conditions for a control period of four days. Trasylol, given intravenously in a dose of 500,000 units over eight hours, failed to affect the output of enzymes over the next two days, or to alter the distribution of bound and soluble enzymes.About 10 years ago, a polypeptide obtained from beef parotid glands ('Trasylol', FBA Pharmaceuticals Ltd), was introduced for the treatment of acute pancreatitis. Its use was based upon its ability to inhibit pancreatic proteolytic enzymes and kinins said to be released during the course of the disease. Although some recent reports indicate that the drug may be of benefit (Hansson and Lenninger, 1967;Kneisel, 1968;Nodine and Greberman, 1968) these trials do not conform to double-blind criteria. Those that do are almost uniform in concluding that Trasylol is without proven effect in the treatment or prophylaxis of acute pancreatitis (Nardi, 1963;Skyring, Singer, and Tornya, 1965;Trapnell, Talbot, and Capper, 1967;Baden, Jordal, Lund, and Zachariae, 1967;Skinner, Corson, and Nardi, 1968;Howat, 1969). Bachrach and Schild (1968) found the drug statistically superior to a placebo but doubted its practical value. Although several reports indicate that the drug protects animals during experimental pancreatitis (McCutcheon and Race,

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Fate of trypsin and chymotrypsin in the human small intestine.

Cited by 49 publications

References 33 publications

A Comparison of Enzyme Activities in Duodenal Aspirate Following Injection of Secretin, Caerulein, and Cholecystokinin

A Comparison of Enzyme Activities in Duodenal Aspirate Following Injection of Secretin, Caerulein, and Cholecystokinin

On the Absorption of Pancreatic Enzymes from the Intestine in Man

Failure of Trasylol to reduce intestinal content of trypsin and chymotrypsin in man

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