Thiolation of polycarbophil enhances its inhibition of intestinal brush border membrane bound aminopeptidase N

2001 ◽  
Vol 90 (11) ◽  
pp. 1907-1914
Author(s):  
Andreas Bernkop‐Schnürch ◽  
Huda Zarti ◽  
Greg F. Walker
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Aminopeptidase N ◽  
Intestinal Brush Border Membrane ◽  
Intestinal Brush Border ◽  
Membrane Bound

Role of intestinal brush border membrane aminopeptidase N in dipeptide transport

FEBS Letters ◽  
1984 ◽  
Vol 171 (2) ◽  
pp. 227-232 ◽  
Author(s):  
V.K. Antonov ◽  
T.I. Vorotyntseva ◽  
L.Ya. Bessmertnaya ◽  
A.G. Mikhailova ◽  
M.I. Zilberman
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Aminopeptidase N ◽  
Intestinal Brush Border Membrane ◽  
Intestinal Brush Border ◽  
Dipeptide Transport

N-linked neutral sugar chains of aminopeptidase N purified from rat small intestinal brush-border membrane

Biochemistry ◽  
1991 ◽  
Vol 30 (37) ◽  
pp. 9102-9110 ◽  
Author(s):  
Seiichi Takasaki ◽  
Roger H. Erickson ◽  
Young S. Kim ◽  
Naohisa Kochibe ◽  
Akira Kobata
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Aminopeptidase N ◽  
Neutral Sugar ◽  
Intestinal Brush Border Membrane ◽  
Intestinal Brush Border ◽  
Small Intestinal ◽  
Sugar Chains

Divalent cations and vitamin B12 uptake by intestinal brush-border membrane vesicles

1980 ◽  
Vol 239 (6) ◽  
pp. G452-G456
Author(s):  
R. C. Beesley ◽  
C. D. Bacheller
Keyword(s):  
Vitamin B12 ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Divalent Cations ◽  
Intrinsic Factor ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Tetraacetic Acid ◽  
Intestinal Brush Border Membrane ◽  
Intestinal Brush Border

Brush-border membrane vesicles from hamster intestine were employed to investigate uptake (binding) of vitamin B12 (B12). Ileal vesicles took up 25 times more B12 than did jejunal vesicles. Uptake of B12 by ileal vesicles was dependent on intrinsic factor (IF) and required Ca2+. Increasing the Ca2+ concentration caused an increase in uptake of B12 reaching a maximum at approximately 8 mM Ca2+. At high Ca2+ concentrations, 6–8 mM, Mg2+ had little effect on uptake of B12. At low Ca2+ concentrations, up to 2 mM, Mg2+ stimulated B12 uptake. Mg2+, Mn2+, and, to a lesser extent, Sr2+ stimulated Ca2+-dependent B12 uptake, but Zn2+, Ba2+, Na+, K+, and La3+ did not. B12 was apparently not metabolized and was bound as IF-B12 complex, which could be removed with (ethylenedinitrilo)tetraacetic acid (EDTA). Our results suggest that two types of divalent cation reactive sites are involved in binding of IF-B12. One is Ca2+ specific. The other is less specific reacting with Mg2+, Mn2+, Sr2+, and perhaps Ca2+ itself, thereby stimulating Ca2+-dependent binding of IF-B12 to its ileal receptor.

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