Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The long-term effects of chain length of dietary fat on intestinal lymphatic transport of alkaline phosphatase were investigated in two patients with chylous ascites due to leakage of intestinal lymph into the peritoneal cavity. Substitution of a medium-chain triglyceride diet for long-chain triglyceride resulted in a parallel fall in triglyceride and the intestinal isoenzyme of alkaline phosphatase in chylous ascites. The concentrations of lymph triglyceride were linearly related to lymph intestinal alkaline phosphatase levels, suggesting a positive relation between absorption of long-chain triglycerides and transport of mucosal alkaline phosphatase into lymph.
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PMID:Influence of carbon chain length of dietary fat on intestinal alkaline phosphatase in chylous ascites. 87 29

1. Using acrylamide gel electrophoresis the serum alkaline phosphatase (ALP) isoenzyme patterns of 204 patients with chronic renal failure have been examined for periods up to 18 months in length. 2. Of those with elevated serum ALP activity the bone isoenzyme was largely responsible. The presence of increasing amounts of the bone isoenzyme even if the total serum ALP activity remains within the normal reference range should also indicate bone pathology. 3. Intestinal alkaline phosphatase was the major serum alkaline phosphatase in 15% of patients on regular haemodialysis and 10% of uraemic patients not on dialysis. The overall incidence of detectable intestinal alkaline phosphatase in those with normal serum ALP activity was 36%. 4. With those patients whose serum ALP activity changed significantly during the investigation this usually reflected changes in the amount of the bone isoenzyme. Patients with abnormal amounts of the intestinal isoenzymes in their serum usually showed little variation in serum ALP activity over the period of the study.
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PMID:Serum alkaline phosphatase isoenzyme patterns in patients with chronic renal failure. 91 6

The serum half-life of feline intestinal alkaline phosphatase (ALP) in the cat was 2 minutes, and that of feline hepatic ALP, 5.8 hours. The feline hepatic ALP could not be identified in the urine of the cats, nor was the clearance rate affected by bilateral nephrectomy. These data indicated the shor serum half-life of hepatic ALP was not a reusult of renal excretion. Since canine hepatic ALP cleared from feline blood at the same rate as the feline hepatic ALP, possibly the discrepancy in hepatic ALP half-life between the species was related to the cats' ability to clear the blood of the enzyme.
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PMID:Serum half-life of intravenously injected intestinal and hepatic alkaline phosphatase isoenzymes in the cat. 93 Nov 46

Pregnant rats were treated with 44, 88 and 176 Medical Research Council munits of thyrocalcitonin (TCT) twice daily during days 10 to 21 of gestation. Nonpregnant rats received the same treatment for 12 days. Administration of TCT to the pregnant rats increased the ash and calcium content of fetal bones and decreased the phosphorus content. The diaphyses were short and contained many persisting enchondral trabeculae and a reduced number of osteoclasts. TCT reduced the fetal intestinal alkaline phosphatase activity but elevated the intestinal calcium-binding protein content. In the pregnant and nonpregnant rats, treatment with TCT resulted in hypocalcemia and hypophosphatemia, and increased the calcium-binding protein content of the duodenal mucosa. In the fetuses, the calcium-binding protein content and alkaline phosphatase activity were higher in the jejunum and ileum than in the duodenum, and were much higher than the values found in adult animals. Our findings indicate that TCT passes through the rat placenta and affects the fetal skeleton and calcium metabolism directly, resulting primarily in decreased bone resorption.
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PMID:Transplacental effects of thyrocalcitonin on intestinal calcium-binding protein, alkaline phosphatase activity and ossification of long bones in rat fetuses. 93 22

This report deals with quantitative and qualitative investigations of alkaline phosphatase in two unrelated infants with the severe infantile form of hypophosphatasia. Both affected infants had no detectable leukocyte alkaline phosphatase activities and both sets of parents and one sibling tended to have low but variable leukocyte enzyme activities. Normal duodenal juice alkaline phosphatase activity was present in the one patient in whom it was measured and a wide range of variation in enzymic activity was observed in the stools. There was no significant difference in the stool enzyme activity between both patients with hypophosphatasia (42.01 +/- 9.77 U) and control infants (40.55 +/- 6.29 U). However, the heterozygous parents had values significantly lower than the control adults (2.10 +/- 0.47 as compared with 19.10 +/- 4.44 U). Intestinal bacteria did not contribute significantly to the stool alkaline phosphatase activity. Enzyme activity was present in the bile of one of the patients and nearly absent in that of the other. Three "inducers" of alkaline phosphatase were given to both patients (phenobarbital, vitamin A, and corticosteroid). No clinical improvement or rise in serum alkaline phosphatase activity was observed during the trial of therapy with these agents. However, a significant increase in the activity of serum acid phosphatase was demonstrated during the course of vitamin A administration, suggesting an in vivo action of vitamin A on the lysosomes through decreasing the stability of the membrane and releasing acid phosphatase to the serum. Quantitative determination of tissue alkaline phosphatases from autopsy tissues was highly variable: no activity was found in bone, lungs, or spleen of either infant; there was a discrepancy in liver and kidney alkaline phosphatase values (zero in one patient and present in the other) and activity was present in the intestinal mucosa of both. Qualitative analysis of kidney, liver, and intestinal alkaline phosphatase revealed some differences between the patients and control subjects in heat inactivation and phenylalanine inhibition (Table 3). Starch gel electrophoresis of the liver preparation of one patient disclosed a single band which had greater mobility than that of six control subjects matched for age. Liver extracts from a premature and from full term newborns showed two bands. The single band of the patient's liver enzyme corresponded to the newborn's fast moving component. In addition, the intestinal enzyme prepared from the same patient had an extra band when compared with age-matched control subjects.
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PMID:Hypophosphatasia: a developmental anomaly of alkaline phosphatase? 93 30

Rat intestinal alkaline phosphatase is an heterogeneous glycoprotein that contains three protein sub-forms separable by electrophoresis. The molecular weight for the glycoprotein (i.e. the average for the three sub-forms) is 157 000-160 000. Three protein sub-forms are detectable on sodium dodecyl sulphate-polyacrylamide gel electrophoresis that migrate at rates corresponding with molecular weights of 64 000, 79 000 and 92 000. Treatment of native alkaline phosphatase with 6 M guanidine - HC1 or buffer at pH 3.0 results in a product with a molecular weight of 78 000 and 70 000, respectively. Thus it is concluded that each of the three sub-forms is a dimer of identical or closely similar subunits. Limited proteolysis results in the production of new enzymically active sub-forms separable by electrophoresis. Using a bacterial protease it is possible to convert intestinal alkaline phosphatase into a form with a molecular weight of 132 000 without causing any significant change in kinetic properties. Electrophoresis of this new form on sodium dodecyl sulphate polyacrylamide gel suggests that it is composed of 66 000-dalton subunits. The native enzyme contains at least 20% by weight of carbohydrate that probably contributes to microheterogeneity of a second degree superimposed on that stemming from the presence of three protein sub-forms. Treatment with various glycosidases has no effect on electrophoretic behaviour, however. It is suggested that the three sub-forms possibly represent different stages of a maturation process that operates by limited proteolysis of a single parent protein.
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PMID:Molecular properties of rat intestinal alkaline phosphatase. 97 5

A zone of alkaline phosphatase activity migrating at about 40 percent of the rate of liver phosphatase in gel electrophoresis has been detected in sera from 2 out of 22 cases of ulcerative colitis and 1 out of 32 cases of Crohn's disease, but in no other specimen from 33 patients with other diseases of the digestive tract. This rare form of alkaline phosphatase was unlike small-intestinal alkaline phosphatase in several properties. Its appearance in association with diseases of the colon suggests that the rare isoenzyme may originate in that organ. However, the slowly migrating alkaline phosphatase was equally prominent in serum specimens taken before and after operation in one patient who underwent a pan-proctocolectomy for the alleviation of uncontrollable ulcerative colitis.
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PMID:Incidence and some properties of an electrophoretically slow form of alkaline phosphatase in sera of patients with diseases of the intestine. 112 26

In the serum of lambs at birth most of the circulating alkaline phosphatase, identified by electrophoretic analysis, was of skeletal origin. Suckling was associated with a rapid increase in activity of intestinal alkaline phosphatase isoenzymes in serum. There was a coincidental increase in level of circulating gamma globulin. Activity of the intestinal isoenzymes in serum began to fall between 15 and 21 h after birth and this fall preceded a fall in serum gamma globulin concentration. The electrophoretic characteristics of the intestinal isoenzymes in serum changed as activity of these isoenzymes increased and then decreased.
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PMID:Isoenzymes of alkaline phosphatase in serum of newly born lambs. 116 17

The autopsy findings of two cases of infantile hypophosphatasia are described and compared with those of 16 previously reported cases. Histochemical and biochemical tissue analysis for alkaline phosphatase showed a marked decrease in activity in liver, kidney, and bones. However, intestinal alkaline phosphatase possessed normal or slightly elevated activity. Nephrocalcinosis is a frequent complication and its development depends on hypercalcemia and length of survival of the patient. Electron microscopic findings are illustrated, and a mechanism for the development of nephrocalcinosis is proposed. For the first time, marked elevations of parathyroid hormone was detected. This finding, coupled with the extreme difficulty in locating the parathyroid glands in cases of hypophosphatasia, is enigmatic. Areas for furture investigation are suggested.
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PMID:Hypophosphatasia-study on two autopsy cases. 119 30

Crystalline human alkaline phosphatase from placenta and intestine was isolated by butanol extraction, acetone precipitation, a heat step (for the placental enzyme), ammonium sulfate precipitation, anion exchange chromatography, gel filtration and crystallisation with ammonium sulfate. Rabbit antibodies showed a partial cross-reaction between both enzymes in double diffusion, quantitative precipitation experiments and in serial precipitin curves. There was no reaction with human alkaline phosphatases from liver, kidney and bone. Three phenotypes of placental alkaline phosphatase with different electrophoretical mobility exhibited identical immunological reactions with their respective antisera. Monospecific antisera were obtained by absorption with crystalline intestinal or placental alkaline phosphatase. These monospecific antisera against the placental or the intestinal alkaline phosphatase can be used for an immunological determination of these two alkaline phosphatases without contamination by other alkaline phosphatases in human serum.
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PMID:Immunological relationship between human placental and intestinal alkaline phosphatase. 120 18


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