Stereospecific, Organ-Specific Inhibition of Intestinal Alkaline Phosphatase

2006 ◽  
Vol 103 (2) ◽  
pp. 951-955 ◽  
Author(s):  
William H. Fishman ◽  
J. H. Kreisher
1982 ◽  
Vol 28 (12) ◽  
pp. 2426-2428 ◽  
Author(s):  
T Komoda ◽  
S Hokari ◽  
M Sonoda ◽  
Y Sakagishi ◽  
T Tamura

Abstract With p-nitrophenyl phosphate as the substrate, there reportedly is no organ-specific inhibition of alkaline phosphatase (EC 3.1.3.1) activity by L-phenylalanine. However, we found that at pH 10.0, with p-nitrophenyl phosphate as the substrate, L-phenylalanine obviously inhibits the alkaline phosphatase isoenzyme from human placenta, whereas there is little if any inhibition of the isoenzyme from human intestine. Because of the differing effects of substrates (p-nitrophenyl phosphate and phenyl phosphate) and their enzymic products (p-nitrophenol and phenol) for L-phenylalanine action on the placental alkaline phosphatase isoenzyme, we suggest that the isoenzyme--inhibitor--substrate complex and the effect of released phosphate on L-phenylalanine inhibition of the isoenzyme activity differ from each other.


Nature ◽  
1963 ◽  
Vol 198 (4881) ◽  
pp. 685-686 ◽  
Author(s):  
WILLIAM H. FISHMAN ◽  
SIDNEY GREEN ◽  
NORMA I. INGLIS

1973 ◽  
Vol 64 (4) ◽  
pp. 599-602 ◽  
Author(s):  
Walter P. Dyck ◽  
George A. Martin ◽  
Charles R. Ratliff

1981 ◽  
Vol 256 (11) ◽  
pp. 5620-5626
Author(s):  
S.T. Yedlin ◽  
G.P. Young ◽  
B. Seetharam ◽  
S. Seetharam ◽  
D.H. Alpers

1988 ◽  
Vol 263 (24) ◽  
pp. 12011-12019 ◽  
Author(s):  
P S Henthorn ◽  
M Raducha ◽  
T Kadesch ◽  
M J Weiss ◽  
H Harris

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