Pancreatic enzyme activities in early life

1980 ◽  
Vol 149 (1) ◽  
pp. 194-200 ◽  
Author(s):  
John F. T. Glasgow ◽  
Hilary C. P. Dinsmore ◽  
Ayesha Molla
Digestion ◽  
1982 ◽  
Vol 24 (1) ◽  
pp. 54-59 ◽  
Author(s):  
G. Isaksson ◽  
I. Lundquist ◽  
I. Ihse

1997 ◽  
Vol 273 (2) ◽  
pp. G553-G558 ◽  
Author(s):  
G. Holtmann ◽  
D. G. Kelly ◽  
B. Sternby ◽  
E. P. DiMagno

The activity of pancreatic enzymes declines during aboral intestinal transit. We tested the hypothesis that survival of pancreatic enzyme activities during intestinal transit is affected by amounts or concentrations of calories, nutrients, bile acids, or pancreatic enzymes entering the segments of the small intestine. An oroileal tube was placed in 26 healthy humans. The tube had duodenal, jejunal, and ileal infusion ports for nonabsorbable markers and aspiration ports in the distal duodenum, distal jejunum, and distal ileum. Four infusates of different proportions of protein, fat, and carbohydrate were infused continuously into the duodenum at 40, 90, and 160 kcal/h. Of the nutrients infused into the proximal duodenum, 21 +/- 3, 51 +/- 7, and 39 +/- 5% of fat, protein, and carbohydrate, respectively, were delivered to the distal duodenum. During duodenoileal transit, lipase, chymotrypsin, amylase, and trypsin lost 71 +/- 5, 63 +/- 5, 43 +/- 7, and 38 +/- 9% of activity, respectively (P < 0.01 vs. distal duodenum). During duodenojejunal transit, the activity of each enzyme decreased more than 35% (P < 0.01 vs. distal duodenum), and infusion of more calories into the duodenum improved survival of all enzymes except trypsin (P < 0.05). During jejunoileal transit, greater amounts and concentrations of calories and carbohydrate improved survival of only lipolytic activity (P < 0.01, P < 0.05, respectively), and loss of lipolytic activity correlated directly with delivery of bile acids (r = 0.56, P = 0.05) and chymotrypsin (r = 0.80, P = 0.001) to the distal jejunum. We conclude that intraluminal nutrients increase survival of enzyme activities in the proximal intestine. After absorption of nutrients, the action of chymotrypsin and bile acids decrease lipolytic activity more than activity of other enzymes.


1992 ◽  
Vol 122 (7) ◽  
pp. 1434-1445 ◽  
Author(s):  
Isabelle Le Huerou-Luron ◽  
Paul Guilloteau ◽  
Catherine Wicker-Planquart ◽  
Jean-Alain Chayvialle ◽  
John Burton ◽  
...  

Pancreas ◽  
1996 ◽  
Vol 12 (4) ◽  
pp. 321-333 ◽  
Author(s):  
Crispin Semakula ◽  
Christina L. Vandewalle ◽  
Christiaan F. H. Van Schravendijk ◽  
Jean-Claude Sodoyez ◽  
Frans C. Schuit ◽  
...  

1943 ◽  
Vol 22 (6) ◽  
pp. 827-838 ◽  
Author(s):  
Sidney Farber ◽  
Harry Shwachman ◽  
Charlotte L. Maddock

1988 ◽  
Vol 118 (7) ◽  
pp. 834-839 ◽  
Author(s):  
Charles G. Lewis ◽  
Otho E. Michaelis ◽  
Chao-Yi Yang ◽  
Nancy Carswell

PEDIATRICS ◽  
1974 ◽  
Vol 54 (2) ◽  
pp. 229-235
Author(s):  
Lynn M. Taussig ◽  
Robert O. Wolf ◽  
Robert E. Woods ◽  
Richard J. Deckelbaum

Amylase isoenzyme patterns were evaluated in serum, urine, and duodenal fluid from 19 patients with cystic fibrosis (CF) and normal subjects. Two thirds of the CF patients with absent pancreatic enzymes lacked a serum pancreatic isoamylase band, while the remainder had a markedly diminished pancreatic band when compared to the salivary isoamylase. In normal sera the pancreatic band is equal to or greater than the salivary band. In all patients with absent enzymes the diagnosis of abnormal pancreatic function could have been made by evaluation of serum isoamylase patterns thereby avoiding duodenal intubation or collection of 72-hour stools for proteolytic enzyme activities. The patients with normal pancreatic enzyme activities had normal serum zymograms. No CF patient had a low total serum amylase concentration. Total duodenal fluid amylase levels may be misleading in the evaluation of pancreatic function since the amylase may be of salivary origin. The advantages of this isoamylase method include (1) simplicity and noninvasiveness, requiring only a small blood sample; (2) specificity for pancreatic function; and (3) independence of pancreatic enzyme medication.


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