Amino Acid Composition of Crystalline Pancreatic Amylase from Swine<sup>1</sup>

Caldwell, M. L.; Dickey, Emma S.; Hanrahan, Virginia M.; Kung, Hsiang-Fu; Kung, Jo-fen Tung; Misko, Mary

doi:10.1021/ja01630a039

Cited by 39 publications

(3 citation statements)

References 1 publication

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Hokin & Hokin (1959) showed, with slices of pigeon pancreas, that all the essential amino acids except methionine were needed for the synthesis of amylase. This could be due to the absence of methionine from the amylase molecule (Meyer, Fischer & Bernfeld, 1947) or its presence in small amounts (Caldwell, Dickey, Hanrahan, Kung, Kung & Misko, 1954). The in vivo results with the intact chickens do not agree with the in vitro results obtained with slices of pigeon pancreas.…”

Section: Discussionmentioning

confidence: 89%

Pancreatic amylase in chickens fed on soya-bean diets

et al. 1966

View full text Add to dashboard Cite

I . The action of raw and heated soya beans on pancreatic function was studied by measuring rhe amylase activity of the pancreases and intestinal contents of intact chickens and of chickens with ileostomies at fasting and after eating, before and after adaptation to heated and raw soya-bean diets, with a methionine supplement and without. 2. The concentration of amylase in the pancreases of 8-week-old chickens eating raw soya-bean diets was lower than that of those eating heated soya-bean diets. These chickens were deficient in methionine; supplementation of the raw soya-bean diet with methionine greatly increased the levels of amylase in the pancreases of such chickens; supplementation of the heated soya-bean diet with methionine increased the levels of amylase in pancreases to a smaller extent. 3. Methionine was less effective in increasing the amylase levels of the pancreases of I r-week-old chickens eating raw soya-bean diets, since at this age the deficiency of methionine was much less pronounced. 4. More amylase activity was found in intestinal contents of chickens eating raw soya-bean diets than in those eating heated soya-bean diets. 5. In vitro studies showed that fractions prepared from raw soya beans, all containing high levels of trypsin inhibitors, stabilized amylase activity despite the active proteolysis of other protein substrates in the same amylase-containing mixtures. 6. CaCl, stabilized amylase activity in vitro in unactivated and activated pancreatic juice as such, and after additions of raw soya beans or their fractions before and after autoclaving. 7. The increased levels of amylase found in the intestinal contents of the chickens eating raw soya beans may represent greater secretion of amylase activity by the pancreas, stabilization of amylase activity by the raw soya bean, or both factors. Interpretation of measurements of amylase activity in the intestinal contents of chickens eating heated or raw soya beans is uncertain. 8. The bearing of this work on current views of the nutritional value of raw and heated soya beans is discussed.Nearly 20 years ago, Chernick, Lepkovksy & Chaikoff (1948) showed that chickens eating raw soya-bean (RS) diets for varying periods of time had pancreases that were hypertrophied and contained higher levels of proteases than did pancreases from corresponding chickens that had eaten heated soya-bean (HS) diets. It was shown later by Applegarth, Furuta & Lepkovsky (1964) that the pancreases of chickens ingesting RS diets were depleted of zymogen granules to a greater extent than corresponding pancreases from chickens ingesting HS diets, indicating a greater release of pancreatic enzymes from the pancreas in response to the ingestion of the RS diets. Chemical analysis supported this histological evidence : lower levels of proteases were found in the pancreases of chickens after eating RS diets than in those of chickens after eating HS diets (Applegarth et al. 1964).The intestinal contents of chickens eating HS and RS diets were examined for corroborative evidenc...

show abstract

Section: Discussionmentioning

confidence: 89%

Pancreatic amylase in chickens fed on soya-bean diets

et al. 1966

View full text Add to dashboard Cite

show abstract

“…However, based on the results in Table 1, there is still less degradation with all three enzymes than what occurs with only amylase or lipase, suggesting enzymatic cross-interference in the solution before interactions occur at the gelatin surface. Due to the prevalence of arginine and lysine in the amino acid compositions of both amylase and lipase, trypsin may be performing additional proteolysis on the nonspecific enzymes in the solution as a result [22,23].…”

Section: Trypsin Impedance Resultsmentioning

confidence: 99%

Gelatin-Enabled Microsensor for Pancreatic Trypsin Sensing

2018

View full text Add to dashboard Cite

Featured Application: Biosensors and bio-detection technologies.Abstract: Digestive health is critically dependent on the secretion of enzymes from the exocrine pancreas to the duodenum via the pancreatic duct. Specifically, pancreatic trypsin is a major protease responsible for breaking down proteins for absorption in the small intestine. Gelatin-based hydrogels, deposited in the form of thin films, have been studied as potential sensor substrates that hydrolyze in the presence of trypsin. In this work, we (1) investigate gelatin as a sensing material; (2) develop a fabrication strategy for coating sensor surfaces; and (3) implement a miniaturized impedance platform for measuring activity levels of pancreatic trypsin. Using impedance spectroscopy, we evaluate gelatin's specificity and rate of degradation when exposed to a combination of pancreatic enzymes in neutral solution representative of the macromolecular heterogeneity present in the duodenal environment. Our findings suggest gelatin's preferential degradation to trypsin compared to enzymes such as lipase and amylase. We further observe their interference with trypsin behavior in equivalent concentrations, reducing film digestion by as much as 83% and 77%, respectively. We achieve film patterns in thicknesses ranging from 300-700 nm, which we coat over interdigitated finger electrode sensors. Finally, we test our sensors over several concentrations to emulate the range of pancreatic secretions. Ultimately, our microsensor will serve as the foundation for developing in situ sensors toward diagnosing pancreatic pathologies.

show abstract

“…Both multiforms of the amylase are physically distinct but structurally related with common active sites (30). Amino acid composition analysis of crystalline enzyme gave a molecular weight of 51,300 + 450 (31). The enzyme also contains five disulfide links to maintain its tertiary structure (32).…”

Section: Literature Reviewmentioning

confidence: 99%

0-(2-hydroxyethyl)-amylose as the substrate of porcine pancreatic [alpha]-amylase action: structural analysis of 0-(2-hydroxyethyl)-maltooligosaccharides

Chan

View full text Add to dashboard Cite

Amino Acid Composition of Crystalline Pancreatic Amylase from Swine¹

Cited by 39 publications

References 1 publication

Pancreatic amylase in chickens fed on soya-bean diets

Pancreatic amylase in chickens fed on soya-bean diets

Gelatin-Enabled Microsensor for Pancreatic Trypsin Sensing

0-(2-hydroxyethyl)-amylose as the substrate of porcine pancreatic [alpha]-amylase action: structural analysis of 0-(2-hydroxyethyl)-maltooligosaccharides

Contact Info

Product

Resources

About

Amino Acid Composition of Crystalline Pancreatic Amylase from Swine1

Cited by 39 publications

References 1 publication

Pancreatic amylase in chickens fed on soya-bean diets

Pancreatic amylase in chickens fed on soya-bean diets

Gelatin-Enabled Microsensor for Pancreatic Trypsin Sensing

0-(2-hydroxyethyl)-amylose as the substrate of porcine pancreatic [alpha]-amylase action: structural analysis of 0-(2-hydroxyethyl)-maltooligosaccharides

Contact Info

Product

Resources

About

Amino Acid Composition of Crystalline Pancreatic Amylase from Swine¹