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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)

We investigated factors influencing alkaline phosphatase activity in the course of developing criteria for the establishment of a standardized method for its determination in human serum at 30 degrees C. The effects of pH, phosphorylatable acceptor (2-amino-2-methyl-1-propanol and diethanolamine), 4-nitrophenyl phosphate, magnesium ion, zinc ion, temperature, volume fraction of specimen, and details of initiation of the reaction have been studied, with use of partly purified enzymes from bone, intestine, liver, and placenta, and sera from patients with a predominant characterized isoenzyme. The purity of the diethanolamine was examined and contaminant monoethanolamine was characterized as a competitive inhibitor. Two sets of recommended conditions are: 2-amino-2-methyl-1-propanol, 0.9 mol/liter; 4-nitrophenyl phosphate, 16 mmol/liter; magnesium ion, 1 mmol/liter; volume fraction of specimen 1/30, and pH30 degrees C 10.5; diethanolamine, 1.8 mol/liter; 4-nitrophenyl phosphate, 18 mmol/liter; magnesium ion, 1 mmol/liter; volume fraction of specimen 1/60, and pH30 degrees C 10.1. Serum is preincubated with all reagents but 4-nitrophenyl phosphate, which is used as the reaction-initiating substrate.
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PMID:Criteria for establishing a standardized method for determining alkaline phosphatase activity in human serum. 2 62

Partially purified alkaline phosphatase (ALP) from canine intestine, liver, and bone were injected into rabbits to elicit anti-canine intestinal, hepatic, and osseous ALP antibodies, respectively. The antibody formed a soluble enzyme-antienzyme complex when directly interacted with the ALP antigen. In order to form an insoluble complex, it was then necessary to interact the initial soluble complex with the goat anti-rabbit gamma-globulin antibody in the 2nd step. Antiintestinal ALP antibody was highly specific and did not cross react with canine hepatic, osseous, splenic, and renal ALP. Antiliver and antibone ALP antibodies, on the other hand, did cross react with hepatic, osseous, splenic, and renal ALP, but not with the intestinal ALP.
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PMID:Immunochemical study of canine intestinal, hepatic, and osseous alkaline phosphatases. 35 71

Changes of alkaline phosphatase in small intestine, liver, kidney, bone and serum of rats administered 100 ppm (890 nM) of Cd2+ in the drinking water were observed during a 12 months period. After 2 weeks of cadmium administration, decreases in bone and small intestine alkaline phosphatases in serum of Cd-exposed rats were observed by a polyacrylamide gradient gel electrophoresis and the alterations continued through the 9th month of administration. At one month, the activities of the alkaline phosphatase fractions, p-1 and p-2, obtained from Sephadex G-200 column gel filtration of bone extracts from Cd-exposed rats were 32% and 43% of those in the controls, respectively, whereas Cd accumulation in the bone was very low (9 nmol/g wet weight). After 3 months, osteoporotic changes of bone and erosion of submucosa layer of the small intestine were observed by light microscopy. Alkaline phosphatase in small intestine of the Cd-exposed rats was 60% of that in the controls after 3 months. At 12 months, the decreased activity of bone alkaline phosphatase in Cd-exposed rats recovered to the same level as activity in the non-exposed rats. Moreover, the activity in kidney of the Cd-exposed rats was 80% of that in the controls. However, histological conversion from osteoporotic to osteomalacic changes in bone and kidney lesions by Cd administration were not observed by light microscopy. Liver alkaline phosphatase activity of the Cd-exposed rats did not change even at 12 months, whereas 1.2 mumol of Cd per g wet weight accumulated in this organ.
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PMID:Effects of orally administered cadmium on alkaline phosphatase isoenzymes in rat tissues. 409 40

Leukocyte alkaline phosphatase (ALP) was subjected to polyacrylamide gradient gel electrophoresis and its observed characteristic mobility compared with the ALP of placenta, intestine, liver, and bone. Comparison runs showed that leukocyte ALP moved more anodal to the origin than the others. Physicochemical differences between the leukocyte and other ALP were examined, based on studies of inhibition by L-phenylalanine, L-homoarginine, urea and EDTA, and of heat inactivation. Leukocyte ALP was inhibited strongly by L-homoarginine and urea but not by L-phenylalanine, which seemed similar to the effect of inhibition of liver and bone ALP. However, heat inactivation appeared to be helpful in distinguishing leukocyte from liver and bone ALP.
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PMID:Physicochemical studies on leukocyte alkaline phosphatase. 619 6

Alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] in placenta, intestine, liver, kidney, bone, and lung from a variety of primate species has been characterized by quantitative inhibition, thermostability, and immunological studies. Characteristic human placental-type alkaline phosphatase occurs in placentas of great apes (chimpanzee and orangutan) but not in placentas of other primates, including gibbon. It is also present in trace amounts in human lung but not in lung or other tissues of various Old and New World monkeys. However, a distinctive alkaline phosphatase resembling it occurs in substantial amounts in lungs from Old World monkeys but not New World monkeys. It appears that duplication of alkaline phosphatase genes and mutations of genetic elements controlling their tissue expression have occurred relatively recently in mammalian evolution.
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PMID:Evolution of alkaline phosphatases in primates. 695 Apr 31

The structural relationship between human alkaline phosphatase isoenzymes from placenta, intestine, liver, bone and kidney was investigated by lectin-binding affinity chromatography. In addition, antibody-binding sites of the enzymes were studied using monospecific antisera against each of the isoenzymes. Evidence is offered for the existence of three classes of alkaline phosphatases: the placental isoenzyme, the intestinal isoenzyme and the liver-bone-kidney-type-isoenzyme: 1. A high affinity to bind to concanavalin A and lentil lectin characterizes the placental isoenzyme in contrast to the other isoenzymes. The intestinal isoenzyme remains totally unbound. The liver-bone-kidney-isoenzyme demonstrates a microheterogeneity with bound and unbound parts. A small unbound fraction can be detected in the placental isoenzyme, also when lentil lectin is used. 2. The placental isoenzyme and the isoenzymes purified from liver, bone and kidney are bound by wheat germ lectin-Sepharose, but not the intestinal isoenzyme. All isoenzymes are eluted as a homogeneous peak. 3. Using Helix pomatia lectin-Sepharose, all isoenzymes are unreactive except a minor fraction of kidney alkaline phosphatase. 4. Antibodies to the placental isoenzyme show a partial cross-reaction with the intestinal isoenzyme, but can be obtained monospecific after absorption. 5. Antibodies to the intestinal isoenzyme show a partial cross-reaction to the placental isoenzyme, respectively, but are monospecific again after absorption. 6. Antibodies to liver, bone or kidney isoenzymes show a complete cross-reaction, but are unreactive with the placental and intestinal isoenzyme; after absorption with a heterologous isoenzyme of this group, no further reaction can be demonstrated with any of the three isoenzymes. Thus, lectin-binding affinity identifies the same isoenzyme classes by their carbohydrate parts, as antibodies presumably do by the protein parts of the isoenzymes. Furthermore, lectin-binding affinity demonstrates a microheterogeneity of the placental isoenzyme with lentil lectin-Sepharose and of the liver-bone-kidney-type-isoenzyme with different lectins.
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PMID:Human alkaline phosphatases. Evidence of three isoenzymes (placental, intestinal and liver-bone-kidney-type) by lectin-binding affinity and immunological specificity. 743 49

There is a clear lack of information on the toxicological risk of dietary intake of cadmium-metallothionein (CdMt). The present study aimed at establishing dose-dependent cadmium (Cd) disposition and to investigate differences in renal toxicity after long-term dietary exposure to CdMt or cadmium chloride (CdCl2) in rats. Male Wistar rats were fed diets containing 0.3, 3, 30, or 90 mg Cd/kg either as CdMt or as CdCl2 for 10 months. In rats fed 30 and 90 mg/kg Cd as CdCl2 the Cd concentrations in intestine, liver, and kidneys were all higher than in rats fed the same doses in the form of CdMt. The kidney/liver Cd concentration ratio was higher with CdMt than with CdCl2. At the lower Cd concentrations (0.3 and 3 mg/kg), no differences in Cd accumulation between CdMt and CdCl2 groups were observed and the kidney/liver Cd ratio was also similar. When based on the amount of CdMt per milligram Cd in the tissue, rats fed CdMt and those fed CdCl2 had a similar relative CdMt concentration in liver and kidney. First signs of renal injury, indicated by an increase of urinary lactate dehydrogenase (LDH) activity, were seen 4 months after exposure to 90 mg/kg Cd as CdCl2. After 8 and 10 months the renal effect of 90 mg/kg Cd as CdCl2 became more pronounced and urinary enzyme activities of LDH, N-acetyl-beta-D-glucosaminidase and alkaline phosphatase were all elevated. The only clinical effect of CdMt at the dose level of 90 mg/kg was a slight increase in urinary gamma-glutamyl transpeptidase activity at 8 and 10 months.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Comparison of renal toxicity after long-term oral administration of cadmium chloride and cadmium-metallothionein in rats. 786 6

Suboptimal protein nutrition during lactation has a negative impact on the digestive function of the small intestine and trophic barrier functions of the large intestine, liver, and kidneys due to significant enzyme deficiency (disaccharidase, peptidase, alkaline phosphatase) in 6-month-old offspring. Changes in enzyme activity in digestive and nondigestive organs play an important role in metabolic disorders promoting the development of "risk diseases" and reducing lifespan.
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PMID:Delayed consequences of protein deficiency during lactation for the development of enzyme systems of digestive and nondigestive organs in offspring. 1212 33

Low protein content in the ration of rat pups during transfer from mixed to definitive nutrition (days 21-30 of life) has a negative impact on digestive function of the small intestine and trophic and barrier functions of the large intestine, liver, and kidneys and increases (sucrase, glycyl-L-leucin dipeptidase) or decreases (alkaline phosphatase, aminopeptidase M, glycyl-L-leucine dipeptidase) enzyme activities in these organs in 6-month-old rats. Protein deficiency during the early ontogeny modulates functioning of the enzyme systems in digestive and non-digestive organs in adult life, which can lead to the development of not only gastrointestinal, but other visceral diseases.
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PMID:Relationship between protein deficiency in the ration of rats during early ontogeny and function of enzyme systems of digestive and non-digestive organs in adult life. 1551 9

The entomopathogenic Autographa californica (Speyer) nucleopolyhedrovirus (AcMNPV) has been genetically modified to increase its speed of kill. The potential adverse effects of a recombinant AcMNPV (AcAaIT) as well as wild type AcMNPV and wild type Spodoptera littoralis NPV (SlNPV) were studied. Cotton plants were treated with these viruses at concentrations that were adjusted to resemble the recommended field application rate (4 x 10(12) PIBs/feddan, feddan = 4,200 m2) and 3rd instar larvae of S. littoralis were allowed to feed on the contaminated plants. SDS-PAGE, ELISA, and DNA analyses were used to confirm that larvae that fed on these plants were virus-infected. Polyhedra that were purified from the infected larvae were subjected to structural protein analysis. A 32 KDa protein was found in polyhedra that were isolated from all of the viruses. Subtle differences were found in the size and abundance of ODV proteins. Antisera against polyhedral proteins isolated from AcAaIT polyhedra were raised in rabbits. The terminal bleeds from rabbits were screened against four coating antigens (i.e., polyhedral proteins from AcAaIT, AcAaIT from field-infected larvae (AcAaIT-field), AcMNPV, and SlNPV) using a two-dimensional titration method with the coated antigen format. Competitive inhibition experiments were conducted in parallel to optimize antibody and coating antigen concentrations for ELISA. The IC50 values for each combination ranged from 1.42 to 163 microg/ml. AcAaIT-derived polyhedrin gave the lowest IC50 value, followed by those of SlNPV, AcAaIT-field, and AcMNPV. The optimized ELISA system showed low cross reactivity for AcMNPV (0.87%), AcAaIT-field (1.2%), and SlNPV (4.0%). Genomic DNAs isolated from AcAaIT that were passaged in larvae of S. littoralis that were reared in the laboratory or field did not show any detectable differences. Albino rats (male and female) that were treated with AcAaIT, AcMNPV or SlNPV (either orally or by intraperitoneal injection at doses of 1 x 10(8) or 1 x 10(7) PIBs/rat, respectively) appeared to be healthy and showed increased body weight at 21 days posttreatment. The effect of virus administration on hematological, serum biochemical, and histopathological parameters were determined. Slight to moderate differences were observed in most of the hematological parameters. Specifically, serum proteins were decreased markedly in female rats treated orally with SlNPV, and in male rats injected with AcAaIT. SDS-PAGE analysis also showed some changes in serum protein profiles. No marked changes in acetylcholine esterase (AChE) activity were found. Changes in serum glucose, alanine aminotransferase (ALT), aspartate aminotransferase (AST), alkaline phosphatase (ALP), bilirubin, creatinin, and urea were also observed. Immunohistochemical observation of tissues from stomach, intestine, liver, kidney, brain, spleen, and lung also showed slight changes. Fish (Tilapia nilotica) were also exposed to AcAaIT, AcMNPV or SlNPV by incorporating each of the viruses into diet (1 x 10(9) PIBs/group). No mortality was found in treated or untreated fish during the experimental period (28 days). Macrophage phagocytic activity of fish head kidney cells increased with time, reaching maximum values at 180 min for both treated and control fish.
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PMID:Biosafety of recombinant and wild type nucleopolyhedroviruses as bioinsecticides. 1761 74


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