Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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 histrochemistry of the adrenal glands was studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). It was impossible to demonstrate any reactivity to UDPG-GT, ADH, alanyl aminopeptidase, leucine aminopeptidase, xilitol (NAD-dependent) dehydrogenase, beta-glucuronidase and aryl-sulfatase in these glands. Total phosphorylase was found in scattered cells of the glomerulosa and adjacent outer fasciculata of one C. penicillata. The dehydrogenases (LDH, G-6-PDH,6-PGDH, NADPH2-TR,ICDH,SDH,NADH2-TR, alpha-GPDH, beta-OHBDH) as well as the hydrolases (except alkaline phosphatase, ATPase, and acetylcholinesterase) showed a stonger reactivity in the cortical part. Some hydrolases (naphthol acetate esterase, acid phosphatase) and cytochrome oxidase were less reactive in the zona glomerulosa, where the dehydrogenases were more abundant. The outer fasciculata and the reticularis also showed a strong dehydrogenase reactivity.
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PMID:Histochemical studies on the adrenal glands of the marmosets (Callithrix jacchus and Callithrix penicillata). 0 44

Nicotinamide adenine dinucleotide phosphate phosphomonoesterase was isolated and partially purified from wheat (Triticum aestivum L. var. Selkirk) leaves. The enzyme had KNADP value of 1.4 X 10(-4) M and a pH optimum of 5.9. In vitro activity of this enzyme was unaffected by precursors of NAD (nicotinamide and nicotinic acid) or cytokinins (kinetin and benzimidazole). However, when detached wheat leaves were treated with solutions of these compounds, the precursors lowered the specific activity while the cytokinins enhanced the activity. It is suggested that spatial separation and compartmentation of the enzyme and its substrate NADP account for the similar effect of benzimidazole on both.
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PMID:Effect of benzimidazole on nicotinamide adenine dinucleotide phosphate phosphomonoesterase activity in wheat leaves. 0 13

The sum of the amounts of NAD + NADH was determined from the same acid tissue extract with the aid of a highly specific radioimmunoassay for 5'-AMP. NAD was converted to 5'-AMP via ADP-ribose by alkaline treatment while NADH was converted first to ADP-ribose by incubation of the acid extract at 25 degrees C followed by alkaline conversion to 5'-AMP. Removal of phosphate groups in NADP and NADPH by treatment of the extracts with alkaline phosphatase extended the procedure to the quantification of NADP(H). When combined with enzymic analyses of the oxidized coenzyme forms, NAD/NADH and NADP/NADPH ratios could also be obtained from the same extracts. The sensitivity of the test allows quantification of pyridine nucleotides in the range of 0.1--10 pmol.
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PMID:Determination by radioimmunoassay of the sum of oxidized and reduced forms of NAD and NADP in picomole quantities from the same acid extract. 4 Jul 93

Ovarian cycle in albino rats was applied to ascertain the problem of the relationship between the salivary and endocrine glands, and also of the extent of participation of individual components of the salivary glands with different functional orientation in the endocrine regulation of individual components of the salivary glands. The content of protein, mucopolysaccharides, DNA, and RNA, the activity of NAD- and NADP-diaphorase, alkaline phosphatase, malate and isocitrate dehydrogenase, alpha-leucine-aminopeptidase was studied. Cytospectrophotometric analysis showed that synchronous changes in the activity of the enzymes under study occurred in all the portions of the salivary glands, depending on the ovarian cycle phases. Of the four successive phases of the cycle the greatest activity of the enzymes and of the protein and mucopolysaccharide content was noted during the proestrus and metaestrus. Different metabolic processes were observed in the salivary ducts in comparison with other parts of the gland; this was apparently connected with peculiarities of the secretion and hormone production.
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PMID:[Quantitative histoenzymologic characteristics of the submaxillary salivary glands of white rats during an ovarian cycle]. 14 76

4-Nitrophenyl and 2-napthyl monoesters of phenylphosphonic acid have been synthesized, and an enzyme catalyzing their hydrolysis was resolved from alkaline phosphatase of a commerical calf intestinal alkaline phosphatase preparation by extensive ion-exchange chromatography, chromatography on L-phenylalanyl-Sepharose with a decreasing gradient of (NH4) 2SO4, and gel filtration. Detergent-solubilized enzyme from fresh bovine intestine was purified after (NH4)2SO4 fractionation by the same technique. The purified enzyme is homogeneous by polyacrylamide gel electrophoresis and sedimentation equilibrium centrifugation. It has a molecular weight of 108,000, contains approximately 21% carbohydrate, and has an amino acid composition considerably different from that reported from alkaline phosphatase from the same tissue. The homogeneous intestinal enzyme, an efficient catalyst of phosphonate ester hydoolysis but not of phosphate monoester hydrolysis, was identified as a 5'-nucleotide phosphodiesterase by its ability to hydrolyze 4-nitrophenyl esters of 5'-TMP but not of 3'-TMP. Also consistent with this identification was the ability of the enzyme to hydrolyze 5'-ATP to 5'-AMP and PPi, NAD+ to 5'-AMP and NMN, TpT to 5'-TMP and thymidine, pApApApA to 5'-AMP, and only the single-stranded portion of tRNA from the 3'-OH end. Snake venom 5'-nucleotide phosphodiesterase also hydrolyzes phosphonate esters, but 3'-nucleotide phosphodiesterase of spleen and cyclic 3',5'-AMP phosphodiesterase do not. Thus, types of phosphodiesterases can be conveniently distinguished by their ability to hydrolyze phosphonate esters. As substrates for 5'-nucleotide phosphodiesterases, phosphonate esters are preferable to the more conventional esters of nucleotides and bis(4-nitrophenyl) phosphate because of their superior stability and ease of synthesis. Furthermore, the rate of hydrolysis of phosphonate esters under saturating conditions is greater than that of the conventional substrates. At substrate concentrations of 1 mM the rates of hydrolysis of phosphonate esters and of nucleotide esters are comparable and both superior to that of bis(4-nitrophenyl) phosphate.
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PMID:Hydrolysis of phosphonate esters catalyzed by 5'-nucleotide phosphodiesterase. 17 Sep 64

Experiments were conducted on young rabbits by the histochemical methods; the activity of NAD-, NADP-diaphorases, cytochromoxidase and alkaline phosphatase was studied in the osteoblasts 3, 6, 12, 24, 48 and 72 hours after combined radiation trauma. It appeared that a bone fracture led to an increase in the level of metabolic and energic processes in the osteoblasts as soon as in 12 hours. Irradiation of the animals depressed the activation (caused by the fracture) of all the enzymes investigated.
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PMID:[Enzymatic activity in the osteoblasts of rabbits following combined trauma]. 17 42

Acute renal failure was induced in male rats by the subcutaneous injectioon of 4 mg HgC12 per kg body weight. Enzyme activities of the proximal tubule were studied histochemically at six time intervals from 15 min to 24 h. The enzyme studied were alkaline phosphatase, 5'-nucleotidase, acid phosphatase, alpha-glycerophosphate dehydrogenase (NAD-independent), malic dehydrogenase, succinic dehydrogenase, latic dehydrogenase, glucose-6-phosphate dehydrogenase and glucose-6-phosphatase. Decreases in activity were observed for alkaline phosphatase and 5'-nucleotidase after 15 min. Acid phosphatase was decreased after 30 min. These three enzymes returned to control levels after 3 h, but malic dehydrogenase and alpha-glycerophosphate dehydrogenase were decreased at this time interval. Succinic dehydrogenase was first decreased after 6 h. The earliest morphological changes detectable by light microscopy were observed in pars recta tubules in the medullary rays after 6 h, a time when all enzymes studied showed widespread decreased activity throughout the proximal tubule. After 24 h, the pars convoluta appeared morphologically normal but the pars recta was necrotic and exhibited calcification, whereas enzyme activity was decreased (absent in some cases) in both pars convoluta and pars recta. These results support the hypothesis that Hg++, when given in a sublethal dose, is associated with early histochemical changes in the brush border of the proximal tubule, which may be related to early changes in sodium reabsorption and to the subsequent development of acute renal failure. The observation that changes in plasma membrane-associated enzymes occur early and prior to alterations in enzymes of mitochondria and the endoplasmic reticulum suggests that Hg++ interacts initially with the plasma membrane.
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PMID:Studies on the pathophysiology of acute renal failure. II. A histochemical study of the proximal tubule of the rat following administration of mercuric chloride. 18 27

Lactate dehydrogenase and alkaline phosphatase activities in the same medium can be determined simulataneously, at 350 and 550 nm, with a vidicon spectrometer. Substrate concentrations and ph have been made optimum for the combined analysis. These conditions result in activities for lactate dehydrogenase that are equivalent to those found by methods in common use, and activites for alkaline phosphatase that are about 31% below the maximum values that could be obtained with its substrate used at the same ph and temperature in the absence of NAD+ and lactate. However, activites measured by the simultaneous analysis were proportional to those obtained by other methods used in clinical laboratories, and the coefficients of variation were 2.3% for lactate dehydrogenase and 3% for alkaline phosphatase.
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PMID:Vidicon spectrometer applied to simultaneous enzyme determinations. 23 3

1. The interaction of NAD+, NADH and various nucleotide analogues with pig kidney alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum) EC 3.1.3.1) has been investigated by kinetic means. Some inhibitors act uncompetitively whereas others markedly increase the slopes of double reciprocal plots suggesting they have some affinity for the free enzyme. 2. The compounds seem to bind to alkaline phosphatase through interactions of their bases with a relatively non-specific region of the enzyme, although it is likely that for those nucleotides having some affinity for the free enzyme there is some attraction between the pyrophosphate backbone and the active site. 3. From studies of the effect of NAD+ and NADH on ATPase activity it was concluded that the substrate inhibition that is characteristic of the ATPase activity of alkaline phosphatase originates from binding of ATP to the site assumed to exist for NAD+ and NADH. The potentiation of NAD+-inhibition of ATPase activity by Mg-2+ is probably a result of the depletion of [ATP-4-] the true substrate. The depletion allows NAD+ to complete more effectively for the active site. 4. Binding of NADH is favoured by protonation of an enzymic group with a pK of approx. 9.0 belonging possibly to a tyrosine residue or a zinc hydrate. 5. A large entropy decrease was found to accompany the binding of NAD+ and NADH to alkaline phosphatase. This may be further evidence of an "induced-fit" mechanism previously suspected because of the synergistic inhibitory effects of adenosine and nicotinamide.
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PMID:Nicotinamide-adenine dinucleotide inhibition of pig kidney alkaline phosphatase. 23 67

1. Rate sedimentation and isopycnic centrifugation were used to analyse the subcellular sites of enzymes in homogenates of goldfish intestinal mucosa. 2. The results allowed the following allocations to be made: carnitine acetyl transferase-mitochondrial and peroxisomal, xanthine dehydrogenase and NAD: alpha-glycerophosphate dehydrogenase soluble phase, NADP: isocitrate dehydrogenase soluble phase and mitochondrial, and 2-naphthyl laurate hydrolase microsomal and/or brush border. 3. Histochemistry confirmed the use of alkaline phosphatase and 1-naphthyl acetate esterase as brush border and microsome markers respectively. 4. Urate oxidase, allantoinase, allantoicase, xanthine oxidase and glycollate/lactate oxidase, activities were undetectable, and 1-naphthyl palmitate hydrolase was present only as a contaminant from pancreas.
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PMID:Intestinal peroxisomes of goldfish (Carassius auratus)--examination for hydrolase, dehydrogenase and carnitine acetyltransferase activities. 31 95


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