Absorption of Galactose by the Rat Small Intestine in Vivo: Proximal—Distal Kinetic Gradients and a New Method to Express Absorption Per Enterocyte

1976 ◽  
Vol 50 (6) ◽  
pp. 499-509 ◽  
Author(s):  
R. M. Batt ◽  
T. J. Peters

1. The absorption in vivo of d-galactose by the rat small intestine has been examined in proximal jejunum and distal ileum by use of a recirculation—perfusion technique. 2. Multiple sequential perfusions over 4 h produced no subsequent functional or morphological damage in the perfused segments. 3. Absorption of galactose from 8 and 64 mmol/l solutions was found to be independent of flow rate over the range 1·0–6·5 ml/min. 4. Galactose absorption in both the jejunum and the ileum exhibited saturation kinetics of the Michaelis—Menten type, and phlorrhizin sensitivity. Sorbose was only absorbed minimally. These observations demonstrate that galactose is absorbed by carrier-mediated transport and that there is no significant passive diffusive component in vivo. 5. Under the stated experimental conditions, the maximum absorptive capacity was 4·5 times greater in the jejunum than in the ileum. The Michaelis constant for galactose was higher in the jejunum than in the ileum. 6. Enterocytes were isolated from perfused segments and quantified by DNA assay with a correction for yield. In this manner, the absorptive capacity per enterocyte was calculated. 7. The maximum absorptive capacity per enterocyte was 3·5 times greater in the jejunum than in the ileum.

1970 ◽  
Vol 38 (3) ◽  
pp. 287-295 ◽  
Author(s):  
I. L. Craft

1. A study of the length, total weight and weight per cm of the small intestine of virgin, pregnant and lactating rats has provided evidence for an increase in intestinal surface area in pregnancy and lactation. 2. Because of such alterations in morphology of the gut the absorption,in vivo, of the substrates studied, glucose and glycine, has been expressed in terms of amount transferred per loop and also per g dry weight of intestine. 3. Using these parameters the results show that pregnancy does not alter the ability of the upper jejunum to absorb glucose and glycine. In lactation there is a significant decrease in the transfer of these substances when expressed per g dry weight of intestine, but not in absolute terms.


1983 ◽  
Vol 49 (1) ◽  
pp. 35-42 ◽  
Author(s):  
D. F. Evered ◽  
J. V. Vadgama

1. Transport ofL-homocitrulline, an amino acid which occurs in milk products, was studied with rat small intestine in vitro and from the human mouth in vivo. Absorption was partially dependent, in both systems, on the presence of sodium ions.2. Metabolic inhibitors decreasedL-homocitrulline uptake across the small intestine. Transport across the intestine did not occur against the concentration gradient but did show saturation kinetics.3. The barbiturate, amytal, did not inhibit buccal absorption. Saturation kinetics were demonstrated.4. Experiments were conducted withL-citrulline, or other amino acids, as possible inhibitors ofL-homocitrulline transport. Results were compatible with Na+-dependent carrier-mediated uptake across the buccal mucosa. Active transport could be involved with the small intestine assuming thatL-homocitrulline has a low affinity for the carrier system.


1979 ◽  
Vol 41 (1) ◽  
pp. 47-51 ◽  
Author(s):  
D. F. Evered ◽  
F. Sadoogh-Abasian

1. The disaccharide lactulose (galactosyl-β-1,4-fructose) was poorly absorbed from rat small intestine in vitro and human mouth in vivo.2. These results confirm indirect clinical evidence of poor absorption from the intestine.3. The presence of calcium ions, or absence of sodium ions, had no effect on lactulose absorption from the buccal cavity.4. The presence of ouabain, or absence of Na+, did not decrease the absorption of lactulose from small intestine.5. It is thought that the mode of transport, in both instances, is by passive diffusion with the concentration gradient.


1975 ◽  
Vol 248 (1) ◽  
pp. 143-149 ◽  
Author(s):  
A E Lane ◽  
D B Silk ◽  
M L Clark

1979 ◽  
Vol 38 (1) ◽  
pp. 267-281
Author(s):  
S.L. Schor ◽  
J. Court

The attachment of cells to collagen has been reported previously to require the presence of serum and the particular serum protein involved in this process, variously known as CIG, CAP or fibronectin, has been isolated. This conclusion that cell attachment to collagen requires serum (or more precisely, fibronectin) is based on experiments measuring the kinetics of cell attachment to films of collagen. We have measured the kinetics of attachment of HeLa and attachment to films of collagen-containing substrata under a variety of experimental conditions and present evidence that the serum-dependent mechanism of cell attachment described by others is actually only the case for films of denatured collagen, while cell attachment to native collagen fibres occurs by a different, serum-independent, mechanism. The possible relevance of these findings to cell-matrix interactions in vivo is discussed.


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