The role of Zn(II) in calf intestinal alkaline phosphatase studied by the influence of chelating agents and chemical modification of histidine residues

Branched-chain amino acids (BCAA) are used as nutritional support for patients with a range of conditions including liver cirrhosis and in-born errors of amino acid metabolism, and they are commonly used “sports” or exercise supplements. The effects of the BCAA on the in-vitro activity of calf intestinal alkaline phosphatase (EC. 3.1.3.1) were studied. All three BCAA were found to be uncompetitive inhibitors of the enzyme with L-leucine being the most potent ([Formula: see text] = 24.9 mmol/L) and L-valine, the least potent ([Formula: see text] = 37 mmol/L). Mixed BCAA are able to act in combination to inhibit the enzyme. Given the important role of intestinal alkaline phosphatase in gut homeostasis, these findings have potential implications for those taking high levels of BCAA as supplements.

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THE BINDING OF ANS TO CALF INTESTINAL ALKALINE PHOSPHATASE

Biochemical Society Transactions ◽

10.1042/bst009244pb ◽

1981 ◽

Vol 9 (2) ◽

pp. 244P-244P

Author(s):

Z. Abdolrazaghi ◽

P. J. Butterworth

Keyword(s):

Alkaline Phosphatase ◽

Intestinal Alkaline Phosphatase ◽

Calf Intestinal Alkaline Phosphatase

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THE ROLE OF ALKALINE PHOSPHATASE IN INTESTINAL ABSORPTION: IV. THE EFFECTS OF VARIOUS PROTEINS ON LEVELS OF THE ENZYME IN INTESTINAL MUCOSA

Canadian Journal of Biochemistry and Physiology ◽

10.1139/y55-013 ◽

1955 ◽

Vol 33 (1) ◽

pp. 89-92 ◽

Cited By ~ 1

Author(s):

Jules Tuba ◽

Nester Dickie

Keyword(s):

Alkaline Phosphatase ◽

Intestinal Absorption ◽

Intestinal Mucosa ◽

Adult Male ◽

Wheat Gluten ◽

Male Rats ◽

Dietary Proteins ◽

Intestinal Alkaline Phosphatase ◽

Egg Albumin

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.

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Stability Properties of Calf Intestinal Alkaline Phosphatase

Progress in Biotechnology - Stability and Stabilization of Biocatalysts, Proceedings of an International Symposium organized under auspices of the Working Party on Applied Biocatalysis of the European Federation of Biotechnology, the University of Cordoba, Spain, and the Spanish Society of Biotechnology ◽

10.1016/s0921-0423(98)80008-7 ◽

1998 ◽

pp. 47-52 ◽

Cited By ~ 1

Author(s):

Ultan McKEON ◽

Brendan O’Connor ◽

Ciarán Ó’fÁgÁin

Keyword(s):

Alkaline Phosphatase ◽

Intestinal Alkaline Phosphatase ◽

Calf Intestinal Alkaline Phosphatase ◽

Stability Properties

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THE ROLE OF ALKALINE PHOSPHATASE IN INTESTINAL ABSORPTION I. THE KINETICS OF PHOSPHATASE ACTION ON VARIOUS SUBSTRATES

Canadian Journal of Medical Sciences ◽

10.1139/cjms53-001 ◽

1953 ◽

Vol 31 (1) ◽

pp. 1-7

Author(s):

Neil B. Madsen ◽

Jules Tuba

Keyword(s):

Alkaline Phosphatase ◽

Average Energy ◽

Inorganic Phosphorus ◽

Intestinal Alkaline Phosphatase ◽

Egg Lecithin ◽

Michaelis Constants ◽

Inhibition Studies ◽

Kinetics Of ◽

Hydrolysis Of

The kinetics of intestinal alkaline phosphatase action on sodium β-glycerophosphate, glucose 6-phosphate, and egg lecithin have been studied and compared. The Michaelis constants indicate that the enzyme shows considerably less affinity for lecithin than for the other two substrates, and the approximate ratio of activity with lecithin, glucose 6-phosphate, and sodium β-glycerophosphate is 11 : 78.5 : 100. The energies of activation for the hydrolysis of the three substrates do not differ appreciably and the average energy of activation is 14,500 calories per gram-mole. The similarity of the energies of activation together with results from inhibition studies indicate that in all probability the same enzyme is responsible for the release of inorganic phosphorus from each of the three substrates.

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