The influence of inclusion of a probiotic in the diet on the development of enzyme activity in the small intestine of the pig

1990 ◽  
Vol 1990 ◽  
pp. 97-97
Author(s):  
G.K. Collington ◽  
D.S. Parker ◽  
D.G. Armstrong ◽  
M. Ellis
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Brush Border ◽  
Microbial Population ◽  
Hydrolase Activity ◽  
Before And After ◽  
Probiotic Preparation

The objective of the present study was to investigate the development of hydrolase enzyme activity at six sites along the small intestine of the pig before and after weaning and the influence inclusion of a probiotic preparation had upon this. The enzymes studied lactase, dipeptidase and tripeptidase are primarily associated with the brush border of the enterocyte cell and expression of hydrolase activity has been shown to be affected by manipulation of the microbial population of the gut.

A Study of Intraluminal Peptide Hydrolase Activity in the Rat

1975 ◽  
Vol 49 (5) ◽  
pp. 523-526
Author(s):  
D. B. A. Silk ◽  
Y. S. Kim
Keyword(s):  
Enzyme Activity ◽  
Brush Border ◽  
Hydrolase Activity ◽  
Soluble Form ◽  
Bacterial Enzymes ◽  
Peptide Hydrolase ◽  
Intestinal Contents

1. Uncentrifuged and centrifuged rat intestinal contents were assayed for peptide hydrolase activity with glycyl-l-phenylalanine (Gly-Phe) and l-phenylalanyl-glycine (Phe-Gly) as substrates in the absence and presence of the intestinal cytosol peptide hydrolase inhibitor p-hydroxymercuribenzoate. 2. Jejunal contents hydrolysed Gly-Phe faster than Phe-Gly. Conversely, ileal contents hydrolysed Phe-Gly faster than Gly-Phe. 3. p-Hydroxymercuribenzoate markedly inhibited jejunal peptide hydrolase activity. There was ten times as much PHMB-resistant activity towards both dipeptides in ileal contents as in jejunal contents. 4. Most of the luminal enzyme activity was present in the supernatants after centrifugation, indicating the luminal enzymes exist in the soluble form. Although the presence of soluble bacterial enzymes cannot be excluded, peptide hydrolase enzymes in jejunal contents have the characteristics of mucosal cytosol enzymes whereas enzymes in ileal contents have the characteristics of mucosal brush border as well as cytosol enzymes.

Mucosal Peptide Hydrolase and Brush-Border Marker Enzyme Activities in Three Regions of the Small Intestine of Rats with Experimental Uraemia

1990 ◽  
Vol 79 (6) ◽  
pp. 663-668 ◽  
Author(s):  
D. J. Haines ◽  
C. H. J. Swan ◽  
J. R. B. Green ◽  
J. F. Woodley
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Intestinal Mucosa ◽  
Brush Border ◽  
Enzyme Activities ◽  
Small Intestinal Mucosa ◽  
Marker Enzyme ◽  
Small Intestinal Transit ◽  
Proximal Small Intestine ◽  
Small Intestinal

1. The activities of nine peptide hydrolases and three non-peptidase brush-border marker enzymes have been quantified in crude homogenates prepared from the proximal, mid and distal regions of small-intestinal mucosa for sham-operated (n = 9) and uraemic (n = 14) rats. Abnormalities in enzyme activities were observed in all regions studied in the uraemic group, although no reduction in food intake occurred. 2. The proximal region of the small intestine from uraemic rats showed a general fall in enzyme activities associated with the brush-border. This fall was combined with a decline in mucosal protein content. In contrast, the mid and distal regions showed increased activity against the dipeptide tyrosyl-glycine. 3. It is proposed that the fall in brush-border enzyme activities in the proximal small intestine of uraemic rats is a response to the increased water intake associated with this, and presumably other, rat models of uraemia. The increased enzyme activity against tyrosyl-glycine found in the mid and distal regions of the small intestine of uraemic rats may be caused by an increased small-intestinal transit rate, but could be an attempt to maximize tyrosine absorption in response to decreased plasma tyrosine levels. 4. This study casts doubt on specific activities being the most useful units of enzyme activity, when measured in crude homogenates prepared from the proximal small intestine of uraemic rats. It also demonstrates that enzyme activities measured at a single site in the small intestine of uraemic rats may not be representative of the enzymatic changes occurring in the small-intestinal mucosa as a whole.

scholarly journals A combined microphysiological-computational omics approach in dietary protein evaluation

2020 ◽  
Vol 4 (1) ◽  
Author(s):  
Paulus G. M. Jochems ◽  
Willem R. Keusters ◽  
Antoine H. P. America ◽  
Pascale C. S. Rietveld ◽  
Shanna Bastiaan-Net ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Brush Border ◽  
Biological Effects ◽  
Whey Protein Concentrate ◽  
World Population ◽  
Biological Efficacy ◽  
Protein Sources ◽  
Immune Parameters ◽  
Peptide Composition ◽  
Brush Border Enzyme

AbstractFood security is under increased pressure due to the ever-growing world population. To tackle this, alternative protein sources need to be evaluated for nutritional value, which requires information on digesta peptide composition in comparison to established protein sources and coupling to biological parameters. Here, a combined experimental and computational approach is presented, which compared seventeen protein sources with cow’s whey protein concentrate (WPC) as the benchmark. In vitro digestion of proteins was followed by proteomics analysis and statistical model-based clustering. Information on digesta peptide composition resulted in 3 cluster groups, primarily driven by the peptide overlap with the benchmark protein WPC. Functional protein data was then incorporated in the computational model after evaluating the effects of eighteen protein digests on intestinal barrier integrity, viability, brush border enzyme activity, and immune parameters using a bioengineered intestine as microphysiological gut system. This resulted in 6 cluster groups. Biological clustering was driven by viability, brush border enzyme activity, and significant differences in immune parameters. Finally, a combination of proteomic and biological efficacy data resulted in 5 clusters groups, driven by a combination of digesta peptide composition and biological effects. The key finding of our holistic approach is that protein source (animal, plant or alternative derived) is not a driving force behind the delivery of bioactive peptides and their biological efficacy.

Hydrolysis and transglycosylation activities of glycosidases from small intestine brush-border membrane vesicles

2021 ◽  
Vol 139 ◽  
pp. 109940
Author(s):  
Lesbia Cristina Julio-Gonzalez ◽  
F. Javier Moreno ◽  
María Luisa Jimeno ◽  
Elisa G. Doyagüez ◽  
Agustín Olano ◽  
...  
Keyword(s):  
Small Intestine ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles

scholarly journals (Na+ + K+)-ATPase and plasma membrane polarity of intestinal epithelial cells: presence of a brush border antigen in the distal large intestine that is immunologically related to beta subunit.

1989 ◽  
Vol 109 (3) ◽  
pp. 1057-1069 ◽  
Author(s):  
A Marxer ◽  
B Stieger ◽  
A Quaroni ◽  
M Kashgarian ◽  
H P Hauri
Keyword(s):  
Monoclonal Antibody ◽  
Small Intestine ◽  
Epithelial Cells ◽  
Brush Border ◽  
Basolateral Membrane ◽  
Apical Cell ◽  
Distal Colon ◽  
Proximal Colon ◽  
Beta Subunit ◽  
Cell Pole

The previously produced monoclonal antibody IEC 1/48 against cultured rat intestinal crypt cells (Quaroni, A., and K. J. Isselbacher. 1981. J. Natl. Cancer Inst. 67:1353-1362) was extensively characterized and found to be directed against the beta subunit of (Na+ + K+)-ATPase as assessed by immunological and enzymatic criteria. Under nondenaturing conditions the antibody precipitated the alpha-beta enzyme complex (98,000 and 48,000 Mr). This probe, together with the monoclonal antibody C 62.4 against the alpha subunit (Kashgarian, M., D. Biemesderfer, M. Caplan, and B. Forbush. 1985. Kidney Int. 28:899-913), was used to localize (Na+ + K+)-ATPase in epithelial cells along the rat intestinal tract by immunofluorescence and immunoelectron microscopy. Both antibodies exclusively labeled the basolateral membrane of small intestine and proximal colon epithelial cells. However, in the distal colon, IEC 1/48, but not C 62.4, also labeled the brush border membrane. The cross-reacting beta-subunit-like antigen on the apical cell pole was tightly associated with isolated brush borders but was apparently devoid of (Na+ + K+)-ATPase activity. Subcellular fractionation of colonocytes in conjunction with limited proteolysis and surface radioiodination of intestinal segments suggested that the cross-reacting antigen in the brush border may be very similar to the beta subunit. The results support the notion that in the small intestine and proximal colon the enzyme subunits are exclusively targeted to the basolateral membrane while in the distal colon nonassembled beta subunit or a beta-subunit-like protein is also transported to the apical cell pole.

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