scholarly journals Dietary Fiber and Phosphorylated Oligosaccharide Protect Small Intestinal Mucosa of Rat from Oxidative Damages in vitro.

1999 ◽  
Vol 46 (7) ◽  
pp. 487-490 ◽  
Author(s):  
Makiko KAWAGUCHI ◽  
Yuko FUJIOKA ◽  
Mikako KISHIMOTO ◽  
Toshiki MATSUURA ◽  
Tomio ICHIKAWA
1997 ◽  
Vol 32 (3) ◽  
pp. 300-305 ◽  
Author(s):  
Satoshi Myojo ◽  
Tomoyuki Tsujikawa ◽  
Masaya Sasaki ◽  
Yoshihide Fujiyama ◽  
Tadao Bamba

2001 ◽  
Vol 33 ◽  
pp. A8
Author(s):  
S. Martucci ◽  
F. Bigai ◽  
J.S. Fraser ◽  
H.J. Ellis ◽  
G.R. Corazza ◽  
...  

1963 ◽  
Vol 18 (2) ◽  
pp. 409-413 ◽  
Author(s):  
Ali Hakim ◽  
R. G. Lester ◽  
N. Lifson

Sheets of dog small intestinal mucosa consisting of only epithelium and lamina propria were mounted for in vitro study. The following transport behavior characteristic of the intestine was found: a) dependence of water transport from isotonic Ringer's fluid on the presence of glucose in the medium, b) water absorption against an osmotic activity difference, c) sensitivity of water transport to small excess hydrostatic pressure on the serosal side, d) uphill glucose movement, and e) chloride impoverishment. Submitted on October 24, 1962


1984 ◽  
Vol 218 (2) ◽  
pp. 459-464 ◽  
Author(s):  
A Jamal ◽  
G L Kellett ◽  
J P Robertson

In common with other phosphofructokinase isoenzymes, phosphofructokinase in the epithelial cells of rat small-intestinal mucosa is activated by fructose 2,6-bisphosphate. However, fructose 2,6-bisphosphate was found not to be present in mucosa as judged by three criteria: (1) chromatography on Sephadex G-25 of crude mucosal extracts from fed rats did not result in a decrease, or indeed any change, in the activity of phosphofructokinase under suboptimal conditions at pH7; (2) ultrafiltrates of mucosal extracts did not possess any acid-labile activating activity when tested against chromatographed liver phosphofructokinase; (3) phosphofructokinase-2 activity was not detectable in mucosal extracts. Furthermore, the perfusion in vitro of isolated loops of jejunum or the incubation of mucosal scrapings from either fed rats or rats starved for 48 h showed that the activity of mucosal phosphofructokinase is not subject to short-term regulation by glucose. These observations are consistent with the view that phosphofructokinase is the rate-limiting enzyme of glycolysis in intestinal mucosa and account for the fact that the rate of glucose utilization by rat small intestine is not very responsive to changes in the concentration of glucose in the lumen.


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