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Enzyme
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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 histologic and histochemical staining characteristics of the triceps brachii (long head), extensor carpi radialis, gluteus medius, vastus lateralis, biceps femoris, semimembranosus, semitendinosus, and extensor digitorum longus muscles of 8 Thoroughbreds, 2 Quarter Horses, 1 Arabian, 1 Paso Fino, and 1 Shetland Pony are described. Muscle fiber morphology, staining distribution and intensity, amount of IM connective tissue, number of IM blood vessels and IM nerves, calcium-activated adenosine triphosphatase activity (CaATPase), percentage of fibertype population, percentage of relative fibertype area, mean fiber diameter, nonspecific esterase activity,
alkaline phosphatase
activity, and acid phosphatase activity were evaluated, using 10 common histochemical and histologic stains. Two fiber types (I, II) and 3 subtypes (IIA, IIB, IIC) were observed, using CaATPase-,
nicotinamide
-adenine dinucleotide-tetrazolium reductase-, periodic acid-Schiff hematoxylin-, and nonspecific esterase-stained frozen serial muscle sections. Type I muscle fibers in general had low CaATPase activity, high oxidative capacity, low glycogen capacity, and low esterase activity. Type IIA muscle fibers had high CaATPase activity, intermediate oxidative capacity, high glycogen concentration, and high esterase activity. Type IIB fibers had high CaATPase activity, low oxidative capacity, high glycogen concentration, and a high esterase activity. Type IIC muscle fibers had high CaATPase activity, high oxidative capacity, variable glycogen concentration, and high esterase activity. Type II (IIA and IIB) muscle fibers predominated in the muscles. The percentage of muscle fiber population, mean minimal muscle fiber diameter, and percentage of relative muscle fiber area were determined for each sampled muscle. Type IIA and IIB muscle fibers predominated in the percentage of muscle fiber population and percentage of relative muscle fiber area. Type IIB muscle fibers had the greatest minimal fiber diameter, type IIA muscle fibers had intermediate minimal fiber diameter, and type I muscle fibers had the smallest minimal fiber diameter. The percentage of relative muscle fiber area was less variable (P less than or equal to 0.05) than the percentage of muscle fiber population. Mean muscle fiber diameter did not significantly differ between breeds. Alkaline and acid phosphatase activities were at low levels in all muscles biopsied and were limited to the IM connective tissue fibrocytes, macrophages, and capillaries.(ABSTRACT TRUNCATED AT 400 WORDS)
...
PMID:Histochemical staining characteristics of normal horse skeletal muscle. 375 94
A method for greatly enhancing the sensitivity of assays employing enzyme labels is described which offers advantages in assays for a wide range of analytes. The principle of the new approach is that the enzyme label gives rise to a catalytic activator for a specific secondary detection system, the activity of which is measured and related back to the amount of label present and thus of the analyte it is being used to determine (C.H. Self, Eur. Pat. Appl. 80303478.4, 15.4.81 exclusively licenced to IQ (Bio) Ltd.). The general principle of enzyme amplification is illustrated by using
alkaline phosphatase
as the labelling enzyme and
nicotinamide
adenine dinucleotide phosphate (NADP) as its substrate. The
nicotinamide
adenine dinucleotide (NAD) formed catalytically activates a strictly NAD specific redox cycle which produces a coloured formazan as the end product. The measured absorbance is at least two orders of magnitude greater than that achieved by conventional methods. The application of this method to immunoassay is demonstrated by a sensitive, rapid and precise assay for human prostatic acid phosphatase (PAP). Some of the many other applications of this methodology are discussed.
...
PMID:A fast highly sensitive colorimetric enzyme immunoassay system demonstrating benefits of enzyme amplification in clinical chemistry. 388 55
1. The inhibition of
alkaline phosphatase
by NAD(+), NADH, adenosine and
nicotinamide
was studied. 2. All of these substances except NAD(+) act as uncompetitive inhibitors, i.e. double-reciprocal plots are parallel. NAD(+), however, is a ;mixed' inhibitor of
alkaline phosphatase
and is less potent than NADH. 3. Inhibition studies with pairs of the inhibitors suggest that, in spite of the difference in type of inhibition, NAD(+) and NADH bind to
alkaline phosphatase
at a common site. Adenosine and
nicotinamide
also seem to bind at the NAD site and the binding of adenosine is facilitated by
nicotinamide
, and vice versa. 4. The facilitation may indicate the occurrence of an induced fit for NAD(+) and NADH. Attempts to desensitize
alkaline phosphatase
to NAD(+) and NADH inhibition by partial denaturation were unsuccessful. 5. The results are discussed in terms of a two-site model in which separate, but interacting, regions exist on the enzyme to accommodate the adenosine and
nicotinamide
moieties of NAD, and a single-site model in which the adenosine part of the molecule is bound preferentially and this interacts with the
nicotinamide
fraction. 6. The activity of
alkaline phosphatase
can be changed fourfold by alteration of the NAD(+)/NADH ratio. This sensitivity to the redox state of the coenzyme could be a means of controlling phosphatase activity.
...
PMID:The inhibition of pig kidney alkaline phosphatase by oxidized or reduced nicotinamide-adenine dinucleotide and related compounds. 435 11
By studying the effects of whole-body X irradiation on phagocytosis, a correlation between the metabolic and bactericidal activities of leukocytes following X irradiation was demonstrated. The total
nicotinamide
adenine dinucleotide (NAD) and
nicotinamide
adenine dinucleotide phosphate (NADP) content of polymorphonuclear neutrolphils (PMN) isolated from irradiated guinea pigs increased significantly when compared to nonirradiated controls. The ratio of unreduced to reduced (NAD) generally increased in PMN isolated from irradiated animals. This occurred with both resting and phagocytizing cells. The ratio of unreduced to reduced NADP of resting PMN isolated from irradiated animals had a tendency to increase. However, in phagocytizing cells a significant decrease in the ratio was noted. The total acid and
alkaline phosphatase
and beta-glucuronidase increased up to about 10 days postirradiation. These lysosomal enzymes returned to approximately normal by the 17th day postirradiation. All three lysosomal enzymes (acid and alkaline phosphatases and beta-glucuronidase) were released from the granules at a significantly faster rate during phagocytosis after irradiation. The bactericidal activities of PMN isolated from irradiated animals gradually decreased, and in some cases increased growth of the organisms was observed. The uptake or association of bacteria with PMN isolated from irradiated animals varied with the postirradiation time. Generally, a correlation with bactericidal activities could be made. The data indicate that the bactericidal system in phagocytes consists of at least two agents, H(2)O(2) and myeloperoxidase.
...
PMID:Role of the phagocyte in host-parasite interactions. 8. Effect of whole-body x-irradiation on nicotinamides, lysosomal enzymes and bactericidal activities of leukocytes during phagocytosis. 438 85
A fixative solution that preserves the activity of some relevant enzymes in muscle histochemistry is described. Portions of human muscle biopsy specimens and selected murine muscles were fresh frozen or placed in the fixative at room temperature for up to 1 month before freezing. Cryostat sections of fresh frozen and fixed frozen tissue were assayed for
nicotinamide
adenine dinucleotide phosphate (NADH)-tetrazolium reductase (NADH), several adenosine triphosphatases (ATPases), myoadenylate deaminase (MD), and phosphorylase. NADH, ATPase, and MD activity were preserved following fixation but phosphorylase was not preserved. Murine spleen and kidney were similarly tested for acid phosphatase (acid phos),
alkaline phosphatase
(alk phos), and nonspecific esterase (NSE). Alk phos activity was preserved but acid phos and NSE activity were significantly reduced following fixation. This fixative is useful in some circumstances for processing or shipping human muscle biopsy specimens and experimental tissues.
...
PMID:A fixative for use in muscle histochemistry. 618 97
A single administration of chlorophos (trichlorophon) solution (600 mg/kg) (LD50) results in vacuolar distrophy appearing in the white rat liver and is especially pronounced in 2-4 days. Thirty minutes after the poisonous chemical is administered, butyrilcholinesterase (BChE) activity is inhibited by 90%, somewhat later oxidation-reduction enzymes activity decreases and
alkaline phosphatase
(APh) activity increases. Cytoplasm of hepatocytes is filled with glycogene and nearly deprived of RNA. Owing to the cytophotometric analysis of the enzymatic activity and the stereologic morphometry method, it has been possible to reveal a certain synchronism in the development of distrophic processes, in a decreasing activity of the oxidation-reduction enzymes and in a disturbed synthesis of glycogene and RNA. On the 6th day after chlorophos has been administered, succinate dehydrogenase and
nicotinamide
-adenine-dinucleotide-phosphate-diaphorase activity, as well as contents and distribution of RNA in hepatocytes reach their control values. BChE and APh activity does not restore. During the whole experiment there is not any statistically significant change in the volumetric part of the sinusoid capillaries and in the stellate reticuloendotheliocytes. Thus, the main effect of chlorophos action is a specific inhibition of ChE, that results in certain structural changes and in changes of the histoenzymatic parameters of the liver.
...
PMID:[Morpho-functional changes in the liver after exposure to cholinesterase inhibitors]. 619 75
The activities of
alkaline phosphatase
and reduced
nicotinamide
adenine dinucleotide (NADH) diaphorase in the principal cells of the guinea pig epididymis were studied histochemically. Alkaline phosphatase activity was absent from the principal cells but was present in the basement membrane of the epididymal epithelium. NADH diaphorase activity was distributed throughout the cytoplasm of the principal cells in each epididymal segment. There was a gradual increase in NADH diaphorase activity from segments 1 through 7. Possible functions of
alkaline phosphatase
and NADH diaphorase in the epididymis are discussed.
...
PMID:Localization of alkaline phosphatase and NADH diaphorase in the principal cells of the guinea pig epididymis. 668 19
The observation that NAD inhibits sodium-dependent phosphate (P) uptake by the luminal brush border membrane (BBM) of the proximal tubule prompted us to examine the specificity and mechanism of this process. Addition of 10(-5) M NAD to the perfusate of isolated perfused rabbit proximal straight tubules inhibited lumen-to-bath P flux by approximately 50%. ADP-ribose had an identical effect, whereas
nicotinamide
had no effect. ADP and 5'-AMP (10(-5) M) also inhibited P flux. Na-dependent uptake of 32P by rabbit BBM vesicles was inhibited by 0.1-0.3 mM NAD, ADP-ribose, ADP, ATP, 5'-AMP, and GDP, which were preincubated with the vesicles for 30 min. The kinetics of inhibition showed an apparent increase in the Km for P but no change in Vmax. These findings are consistent with "competitive inhibition." The nucleotides inhibited P uptake even when BBM
alkaline phosphatase
was inhibited by 96% with 10 mM theophylline. Evidence of nonspecific phosphatase activity was present, since incubation of BBM with 0.1 mM solution of nucleotides for 30 min resulted in an elevation of free P in the medium of approximately 0.15-0.22 mM. Correction of 32P specific activity for this change resulted in values for Km and Vmax that were not significantly different from control. The "competitive inhibition" could thus be ascribed to an isotope-dilution effect. There was no evidence to suggest that NAD caused ADP-ribosylation of the luminal membrane. These studies indicate that adenine and guanine nucleotides do not inhibit P transport by a direct action on the luminal membrane of the proximal tubule but do inhibit lumen-to-bath P flux in isolated perfused proximal tubules at concentrations of 10(-5) M. Since there is no direct inhibitory effect of these compounds at the level of the BBM, it is possible that they inhibit P transport by altering some event subsequent to the transfer of P across the luminal membrane.
...
PMID:Nucleotide inhibition of phosphate transport in the renal proximal tubule. 688 41
Tendon tissue of eleven athletes suffering from insertion tendopathy and of two controls was examined. Part of the tissue was prepared for routine light microscopy, a part for enzyme histochemical staining of
Nicotinamide
-adenine-dinudeotide-diaphorase (NADP-diaphorase), lactate dehydrogenase (LDH), beta-glucuronidase and
alkaline phosphatase
. Small pieces of tissue were also prepared for electron microscopic examination. The removed tissue was edematous and mushy. The normally densely packed parallel or interwoven collagen bundles were loosened by edema, focal necrosis or hemorrhage. Infiltration of fatty tissue and granulation tissue was also present. The amount of acid mucopolysaccharides was markedly increased. The histochemical studies showed strong enzyme activity of NADP-diaphorase and LDH in normal tendon tissue as well as around areas of degeneration and in granulation tissue. beta-Glucuronidase and
alkaline phosphatase
was present, but in general with lesser activity than the above enzymes. The electron microscopic examination revealed marked degeneration of the fiber systems, focal necrosis, deposit of amorphous masses and mucopolysaccharides and focal mineralisation. The reparative zones showed proliferating capillaries, often with a collapsed lumen and prominent endothelial cells and basement membranes.
...
PMID:Insertion tendopathy in athletes. A light microscopic, histochemical and electron microscopic examination. 712 23
Polymorphonuclear leukocytes were isolated from the peripheral blood of rabbits by Ficoll-Hypaque centrifugation followed by dextran sedimentation. The granulocytes were homogenized in isotonic sucrose and subjected to analytical subcellular fractionation by sucrose density gradient centrifugation. Leucine aminopeptidase, when assayed with L-leucine-7-amido-4-methyl-coumarin as substrate, showed a similar distribution to N-acetyl-beta-glucosaminidase and thus is localized to the tertiary granules. There was no leucine aminopeptidase associated with the plasma membrane of these cells. Further experiments with purified plasma membranes and inhibitor studies using diazotized sulphanilic acid further confirmed that leucine aminopeptidase had a purely intracellular localization.
Vitamin B
-12 binding protein showed a similar localization to
alkaline phosphatase
indicating that, as in human polymorphonuclear leukocytes, vitamin B-12 binding protein is located to the specific granules.
...
PMID:Localization of leucine aminopeptidase and vitamin B-12 binding protein in rabbit peripheral blood polymorphonuclear leukocytes. 715 Jun 59
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