scholarly journals Studies on alkaline phosphatase. Phosphorylation of calf intestinal alkaline phosphatase by 32P-labelled pyrophosphate

1968 ◽  
Vol 107 (2) ◽  
pp. 279-283 ◽  
Author(s):  
H N Fernley ◽  
Sylvia Bisaz

1. A purified preparation of alkaline phosphatase from calf-intestinal mucosa was phosphorylated by 32P-labelled PPi at a serine residue on the enzyme. Under the conditions employed, up to 0·15μm-labelled sites were obtained from 1μm-[32P]PPi. 2. The phosphorylated enzyme was labile, the rate of dephosphorylation being similar to the overall rate of substrate hydrolysis. 3. A stopped-flow technique was used to determine the number of phosphomonoesterase active sites, which agreed with the number of 32P-labelled sites. 4. It is concluded that calf-intestinal alkaline phosphatase is both a phosphomonoesterase and a pyrophosphatase.

1955 ◽  
Vol 33 (1) ◽  
pp. 89-92 ◽  
Author(s):  
Jules Tuba ◽  
Nester Dickie

Fasted adult male rats were used to study the effect of dietary proteins on intestinal alkaline phosphatase. Groups of animals were offered one of several proteins; lactalbumin, egg albumin, zein, gelatin, wheat gluten, casein, and vitellin. Control animals had cellulose fed to them. The rats were sacrificed six hours after they were given the different diets. Alkaline phosphatase determinations with intestinal homogenates indicated that the two phosphoproteins, casein and vitellin, elevated levels of the enzyme significantly above fasting levels. Possible interpretations of these findings are discussed.


1983 ◽  
Vol 66 (3) ◽  
pp. 871-879 ◽  
Author(s):  
Plato Portmann ◽  
Hubert Schaller ◽  
Geneviève Leva ◽  
Werner Venetz ◽  
Thomas Müller

2001 ◽  
Vol 36 (8) ◽  
pp. 960-972 ◽  
Author(s):  
Renate Bublitz ◽  
Horst Hoppe ◽  
Gerhard A. Cumme ◽  
Mariana Thiele ◽  
Adrian Attey ◽  
...  

1982 ◽  
Vol 65 (8) ◽  
pp. 2668-2681 ◽  
Author(s):  
Plato Portmann ◽  
Andreas Jörg ◽  
Kurt Furrer ◽  
Hans-Sepp Walker ◽  
Peter Leuthard ◽  
...  

1954 ◽  
Vol 32 (1) ◽  
pp. 621-624 ◽  
Author(s):  
Jules Tuba ◽  
Nestor Dickie

Adult male rats were deprived of food for five days. Various groups of these animals were then offered cellulose or cellulose mixed with one of seven other carbohydrates. Six hours after food was placed before them, the animals were killed by decapitation, and a portion of the intestine from each rat was homogenized. Intestinal alkaline phosphatase estimations indicated (1) that the activity of the enzyme was increased significantly by the ingestion of glucose, galactose, fructose, and mannose, whereas (2) there was not a statistically significant elevation of the enzyme level in those animals which had been fed cellulose, arabinose, xylose, or sucrose. This would appear to suggest that alkaline phosphatase is involved in the intestinal absorption of some monosaccharides.


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