Dot blot chemiluminescence assay for studying food protein binding to small intestinal brush border membranes in vitro

1997 ◽  
Vol 34 (3) ◽  
pp. 189-203 ◽  
Author(s):  
Gabriele Bolte ◽  
Margarete Knauss ◽  
Irene Metzdorf ◽  
Martin Stern
Keyword(s):  
Protein Binding ◽  
Brush Border ◽  
Food Protein ◽  
Dot Blot ◽  
Brush Border Membranes ◽  
Chemiluminescence Assay ◽  
Intestinal Brush Border ◽  
Small Intestinal

In vitro Gastrointestinal Models for Prebiotic Carbohydrates: A Critical Review

2019 ◽  
Vol 25 (32) ◽  
pp. 3478-3483 ◽  
Author(s):  
Oswaldo Hernandez-Hernandez
Keyword(s):  
Small Intestine ◽  
Gastrointestinal Tract ◽  
Brush Border ◽  
Critical Review ◽  
In Vitro Digestibility ◽  
Human Gastrointestinal Tract ◽  
Intestinal Brush Border ◽  
Small Intestinal ◽  
Existing Data

Background: In the last decade, various consortia and companies have created standardized digestion protocols and gastrointestinal simulators, such as the protocol proposed by the INFOGEST Consortium, the simulator SHIME, the simulator simgi®, the TIM, etc. Most of them claim to simulate the entire human gastrointestinal tract. However, few results have been reported on the use of these systems with potential prebiotic carbohydrates. Methods: This critical review addresses the existing data on the analysis of prebiotic carbohydrates by different in vitro gastrointestinal simulators, the lack of parameters that could affect the results, and recommendations for their enhancement. Results: According to the reviewed data, there is a lack of a realistic approximation of the small intestinal conditions, mainly because of the absence of hydrolytic conditions, such as the presence of small intestinal brush border carbohydrases that can affect the digestibility of different carbohydrates, including prebiotics. Conclusion: There is a necessity to standardize and enhance the small intestine simulators to study the in vitro digestibility of carbohydrates.

scholarly journals Enhanced Peptide-Binding Capacities of Small Intestinal Brush Border Membranes in Celiac Disease

1999 ◽  
Vol 46 (6) ◽  
pp. 666-666 ◽  
Author(s):  
Gabriele Bolte ◽  
Werner Seilmeier ◽  
Herbert Wieser ◽  
Kati Holm ◽  
Karin Beuermann ◽  
...  
Keyword(s):  
Celiac Disease ◽  
Brush Border ◽  
Peptide Binding ◽  
Brush Border Membranes ◽  
Intestinal Brush Border ◽  
Small Intestinal

Characterization and modulation of rat small intestinal brush-border membrane transbilayer fluidity

1991 ◽  
Vol 260 (4) ◽  
pp. G586-G594
Author(s):  
P. K. Dudeja ◽  
R. K. Wali ◽  
J. M. Harig ◽  
T. A. Brasitus
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Leucine Aminopeptidase ◽  
Aminopeptidase Activity ◽  
Intestinal Brush Border Membrane ◽  
Intestinal Brush Border ◽  
Leucine Transport ◽  
Small Intestinal

In the present experiments, selective quenching by trinitrophenyl groups as well as steady-state fluorescence polarization and differential polarized phase fluorescence techniques, using three different lipid soluble fluorophores, were used to directly examine the fluidity of the exofacial and cytofacial leaflets of rat small intestinal brush-border membranes. These studies revealed that the fluidity of the exofacial hemileaflet was greater than the cytofacial hemileaflet. Differences in the distribution of phosphatidylcholine and phosphatidylethanolamine, as assessed by phospholipase A2 treatment and trinitrophenylation of aminophospholipids, were, at least partially, responsible for the asymmetrical fluidity of the hemileaflets. Moreover, in vitro addition of benzyl alcohol (final concn 25 mM) preferentially fluidized the exofacial leaflet and concomitantly decreased leucine aminopeptidase activity but did not affect the activities of maltase, sucrase, alkaline phosphatase, or gamma-glutamyltranspeptidase. In vivo addition of the membrane-mobility agent 2-(2-methoxyethoxy)ethyl 8-(cis-2-n-octylcyclopropyl)octanate] (A2C) (final concn 7.5 microM) preferentially fluidized the cytofacial leaflet and increased Na(+)-gradient-dependent D-glucose transport but not Na(+)-gradient-dependent L-leucine transport.

Variability of soya-bean lectin binding sites in the brush border membranes of calf intestinal epithelium

1989 ◽  
Vol 49 (2) ◽  
pp. 229-232 ◽  
Author(s):  
H. G. C. J. M. Hendriks ◽  
J. F. J. G. Koninkx ◽  
M. Draaijer ◽  
J. E. van Dijk ◽  
J. A. M. Raaijmakers ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Brush Border ◽  
Binding Sites ◽  
Lectin Binding ◽  
Soya Bean ◽  
Veal Calves ◽  
Brush Border Membranes ◽  
Intestinal Brush Border ◽  
Small Intestinal ◽  
Lectin Binding Sites

ABSTRACTAn enzyme-linked lectin sorbent assay (ELLSA) has been used to determine quantitatively the amount of soya-bean agglutinin (SBA) binding sites in and the sialic acid contents of small intestinal brush border membranes (BBM) of a group of 14 clinically healthy veal calves. Computer analysis of the results indicated 704 (s.e. 27) nmol SBA binding sites per mg of BBM protein with a Kj of 2·63 (s.e. 0·15) × 10-5mol/l; the sialic acid contents were 2·67 (s.e. 0·43) mg/g BBM protein. We could not demonstrate a correlation between the amount of binding sites and the sialic acid contents of the BBM.Incubation with neuraminidase did not alter the number of SBA binding sites.

Regional specificity of iron uptake by small intestinal brush-border membranes from normal and iron-deficient mice

1985 ◽  
Vol 248 (3) ◽  
pp. G376-G379 ◽  
Author(s):  
A. Muir ◽  
U. Hopfer
Keyword(s):  
Brush Border ◽  
Iron Uptake ◽  
Iron Absorption ◽  
Membrane Vesicles ◽  
Soluble Form ◽  
Brush Border Membranes ◽  
Intestinal Brush Border ◽  
Iron Deficient ◽  
Small Intestinal ◽  
Deficient Mice

Fe(II)-ascorbate uptake by purified small intestinal brush-border membrane vesicles prepared from proximal and distal segments was studied in normal and iron-deficient mice. Iron was maintained in a reduced, soluble form by a 20-fold excess of ascorbate at a physiological pH of 7.2-7.4. In normal mice, iron uptake by proximal membrane vesicles was three- to fourfold greater (approximately 1,700 pmol/mg prot) than from distal segments (approximately 500 pmol/mg prot). In iron-deficient mice, uptake of Fe(II) was also greater in proximal membranes (approximately 3,200 pmol/mg prot) than uptake from distal segments (approximately 350 pmol/mg prot), and the regional difference was almost 10-fold, without any change in distal segmental iron uptake. These results are consistent with the pattern of intestinal iron absorption in iron-replete and iron-deficient animals and indicate that regulatory changes in proximal intestinal brush-border membranes may account for the increased iron absorption known to occur in iron deficiency.

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