scholarly journals Oligopeptidases of brush border membranes of rat small intestinal mucosal cells

1972 ◽  
Vol 227 (2) ◽  
pp. 377-394 ◽  
Author(s):  
M. Fujita ◽  
D. S. Parsons ◽  
Fenella Wojnarowska
Keyword(s):  
Brush Border ◽  
Brush Border Membranes ◽  
Mucosal Cells ◽  
Small Intestinal ◽  
Intestinal Mucosal Cells

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

Demonstration of methionine synthetase in intestinal mucosal cells of the rat

1985 ◽  
Vol 69 (3) ◽  
pp. 287-292 ◽  
Author(s):  
J. N. Keating ◽  
D. G. Weir ◽  
J. M. Scott
Keyword(s):  
Crypt Cell ◽  
Cell Populations ◽  
Buffer System ◽  
Mucosal Cell ◽  
Mucosal Cells ◽  
Rat Duodenum ◽  
Small Intestinal ◽  
Intestinal Mucosal Cells ◽  
Crypt Cells

1. Methionine synthetase was measured in the mucosal cells of the rat duodenum, jejunum and ileum by a previously employed method for mucosal cell isolation. No activity was found in these cells. 2. When a dual buffer system for the isolation of villous and crypt cell population was substituted, however, methionine synthetase was found to be active in the duodenum, jejunum and ileum, both in the villous and crypt cell populations. The activity was significantly higher in the crypt cells than in the villous cells throughout the intestine, and higher levels were found in the ileum than in the duodenum or jejunum. 3. As had been previously reported for the rat liver, nitrous oxide in vivo reduced the enzyme activity in both the villous and crypt cell populations, suggesting a role in vivo for the enzyme. We conclude that methionine synthetase is both present and active in the small intestinal mucosal cells of the rat.

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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