Pancreatic Enzymes of the Spiny Pacific Dogfish. II. Procarboxypeptidase B and Carboxypeptidase B*

Biochemistry ◽  
1966 ◽  
Vol 5 (12) ◽  
pp. 4137-4145 ◽  
Author(s):  
James W. Prahl ◽  
Hans Neurath
PEDIATRICS ◽  
1980 ◽  
Vol 66 (4) ◽  
pp. 556-560 ◽  
Author(s):  
Emanuel Lebenthal ◽  
P. C. Lee

The ability of newborns to digest proteins, fats, and carbohydrates depends, to a large extent, on their level of exocrine pancreatic function. Building on the limited published data, we studied pancreatic enzyme activities in the duodenal fluid and the response of the exocrine pancreas to secretogogues in 15 premature and full-term infants at birth and at 30 days of age. We compared these findings to those obtained from identical studies of 17 children age 2 years and above. In addition, we measured the pancreatic exopeptidase, carboxypeptidase B, in relation to other pancreatic enzymes. The duodenal fluid of newborns and infants contained no amylase and negligible lipase. Carboxypeptidase B levels were also low compared to those in the older children. In contrast, chymotrypsin activity in infants was about 50% to 60% of level found in the older children. Trypsin activity, the highest of all enzymes measured, was about the same in both newborns and older children, with a transient increase at 30 days. Administration of pancreozymin had no effect on pancreatic enzymes in the duodenal fluid of newborns and a slight effect on 1-month-old infants. But by age 2 years, a full response of the pancreas to pancreozymin was evident. In infants and newborns, responses to secretin were poor. Thus, the secretory response of the human pancreas to secretogogues, absent or minimal at birth, is acquired during the postnatal period.


Author(s):  
Kenjiro Yasuda

Localization of amylase,chymotrypsinogen and trypsinogen in pancreas was demonstrated by Yasuda and Coons (1966), by using fluorescent antibody method. These enzymes were naturally found in the zymogen granules. Among them, amylase showed a diffuse localization around the nucleus, in addition to the zymogen granules. Using ferritin antibody method, scattered ferritin granules were also found around the Golgi area (Yasuda et al.,1967). The recent advance in the tissue preparation enables the antigen to be localized in the ultrathin frozen sections, by applying the labeled antibodies onto the sections instead of staining the tissue en bloc.The present study deals with the comparison of the localization of amylase and lipase demonstrated by applying the bismuth-labeled, peroxidase-labeled and ferritin-labeled antibody methods on the ultrathin frozen sections of pancreas, and on the blocks of the same tissue.


1960 ◽  
Vol 38 (6) ◽  
pp. 954-956 ◽  
Author(s):  
Allan E. Dumont ◽  
John H. Mulholland

1958 ◽  
Vol 231 (1) ◽  
pp. 393-401 ◽  
Author(s):  
Jules A. Gladner ◽  
J.E. Folk
Keyword(s):  

1958 ◽  
Vol 231 (1) ◽  
pp. 379-391
Author(s):  
J.E. Folk ◽  
Jules A. Gladner
Keyword(s):  

2020 ◽  
Vol 8 (5) ◽  
pp. 1728-1732.e1 ◽  
Author(s):  
Cosby A. Stone ◽  
Shailesh Choudhary ◽  
Megan F. Patterson ◽  
Christine R.F. Rukasin ◽  
David T. Coleman ◽  
...  

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.


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