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)

A sensitive assay for hyaluronidase was developed using as a substrate, hyaluronic acid insolubilized on polystyrene microtest plates. Hyaluronic acid was measured exploiting the fact that it can bind immune complexes made up with hyaluronectin and alkaline phosphatase-conjugated anti-hyaluronectin antibodies. Hyaluronidase was detected in both cell line culture media. Optimum pH was between 3.25 and 3.75. Sodium chloride dependence was absolute, and the optimum concentration of sodium chloride was between 0.2 and 0.3 M. The activity was not affected by dialysis, and was suppressed by a 5 minute heating at 50 degrees C or by protease treatment. The molecular weight was 68 K as determined by gel permeation chromatography. The results are close to those reported for human lysosomal hyaluronidase.
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PMID:[Characterization of lysosomal-type hyaluronidase in the culture medium of 2 cell lines derived from human hepatomas]. 301 17

Serum concentrations of total proteins, albumin, glucose, alkaline phosphatase, alanine transaminase, aspartate transaminase, gamma-glutamyltransferase, lactate dehydrogenase, creatine kinase, urea, creatinine, total calcium, ionised calcium, total magnesium, sodium chloride, potassium, phosphorus, cortisol, parathormone, 25-hydroxy-VitD3 and insulin as well as the results of haematological investigations in Cape vultures (n = 10) are presented.
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PMID:Serum biochemical and haematological parameters in the Cape vulture Gyps coprotheres. 350 9

1. Benzyl phosphonates were prepared and their potentialities as chromophoric reagents for the exploration of the substrate-binding site of Escherichia coli alkaline phosphatase were investigated. 4-Nitrobenzylphosphonate is a competitive inhibitor of the enzyme. 2-Hydroxy-5-nitrobenzylphosphonate changes its spectrum on binding to the enzyme. This spectral change is reversed when the phosphonate is displaced from the enzyme by substrate. 2. The kinetics of the reaction of 2-hydroxy-5-nitrophenylphosphonate were studied by the stopped-flow and the temperature-jump techniques. It was found that the combination of the phosphonate with the enzyme occurred in two successive and reversible steps: enzyme-phosphonate complex-formation followed by rearrangement of the complex. The spectral change is associated with the rearrangement. At pH8 in 1m-sodium chloride at 22 degrees the rate constant is 167sec.(-1) for the rearrangement of the initially formed binary complex and is 18sec.(-1) for the reverse process. 3. It has previously been proposed that the reactions of phosphatase with its substrates include a distinct step between enzyme-substrate combination and chemical catalysis. The rate constant involved could be predicted but not measured from experiments with substrates. The value for the rate constant measured from the rate of the enzyme-phosphonate rearrangement is in excellent agreement with the predicted value. A model for the reaction mechanism is proposed that includes a conformation change in response to phosphate ester binding before phosphate transfer from substrate to enzyme.
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PMID:A substate-induced conformation change in the reaction of alkaline phosphatase from Escherichia coli. 489 58

The production of the bacteriocin ulceracin 378 by Corynebacterium ulcerans 378 was demonstrated during the growth of the organism on solid medium. Ulceracin 378 was not found in broth cultures and could not be extracted from the organisms by various solvents and salt solutions. Ulceracin 378 was not inducible by UV irradiation or mitomycin C treatments. Ulceracin 378 was active against all of the C. ulcerans strains tested and some related species, but it was not autoinhibitory. The active material was not phage related and was extracted from cultures grown on semisolid media composed of proteose peptone, Tween 80, Casamino Acids, glycerol, and sodium chloride. The yield was significantly reduced by either increasing the agar concentration or omitting Tween 80. Ulceracin 378 was resistant to DNase, RNase, phospholipases C and D, and alkaline phosphatase but was susceptible to proteolytic enzymes. This suggests that the active principle of ulceracin is protein in nature. Ulceracin 378 was partially purified by ammonium sulfate fractionation, dialysis, and chromatography on DEAE-cellulose.
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PMID:Production of a bacteriocin, ulceracin 378, by Corynebacterium ulcerans. 668 39

Two 4-week trials were conducted to determine the role of sodium chloride (salt) on field rickets in poults. A comparison of added dietary salt at 0, .075, .10, .25, and .45% to a corn-soy basal with .103% salt showed significant differences (P less than .05) in body weight gains, blood calcium, magnesium and sodium, feed conversion, and adrenal gland weights among the treatments. Mortality and abnormal bone scores decreased with increasing salt. When sodium was added to the basal diet as a single element for the poults at either 0, .09, .10, .11, and .12%, or chloride at 0, .009, .01, .02, and .03% in comparison to a control group with .20% sodium and .30% chloride, significant differences were found in weekly gain, bone ash, bone breaking strength, tibia weight/body weight, and serum alkaline phosphatase levels between the sodium, chloride, and the combined element groups. Bone abnormality scores decreased with increasing levels of both sodium and chloride in diets.
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PMID:Effect of low salt, sodium, and chloride levels in poult rations on growth, bone development, and related factors. 683 8

The multicomponent solution, containing 15% of glycerol, 4.5% of proteins, 0.9% of sodium chloride, 0.33% of potassium chloride and water for injections, was proposed. The ferments activity (aminotransferases, cholinesterase, aldolase, alkaline phosphatase), blood coagulating system state (the prothrombin level, plasma tolerance, her recalcification time), the mineral elements contents (potassium, sodium, calcium), the contents of protein and its fractions in blood before and after an acute blood loss compensation with the multicomponent solution, and also its influence on the animals organism in prolonged daily (during 30 days) intravenous injection were studied. The combination of components in the solution permit to store the studying indexes on level close to initial; if the loss of blood compensates in the first hours, high survival of animals is insured. Negative reactions of organism while prolonged intravenous injection of the multicomponent solution are not revealed.
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PMID:[Use of glycerin as a component of the solution in treating acute hemorrhage]. 760 2

The influence of intestinal metaplasia on gastric cancer induction was examined in five-week-old male Wistar:Crj rats. The animals were first treated with two 10 Gy doses of X-rays to the gastric region at a 3-day interval (total 20 Gy) and then, starting two months after the irradiation, received 100 ppm N-methyl-N-nitrosourea (MNU) in their drinking water for 15 weeks. Thereafter they were maintained for 37 weeks with or without a dietary 1% sodium chloride (NaCl) supplement. The incidences of gastric adenocarcinomas in the MNU or MNU plus NaCl groups were significantly higher than in animals receiving X-rays plus MNU with or without NaCl. Intestinal metaplasias and the numbers of alkaline phosphatase (ALP)-positive foci were significantly increased in the X-ray irradiation groups but the numbers of ALP-positive foci were not increased with or without 1% NaCl. An inverse relationship between incidences of gastric tumors and intestinal metaplasias was apparent. The present experiment thus showed that the presence of intestinal metaplasia does not exert a positive influence on induction of gastric neoplasia by MNU in the rat.
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PMID:Lack of any positive effect of intestinal metaplasia on induction of gastric tumors in Wistar rats treated with N-methyl-N-nitrosourea in their drinking water. 796 Nov 16

As shown in experiments on 40 Chinchilla male rabbits, sinusoidal modulated currents (SMC) and ultrasound (US) are able to enhance bioelectrical activity of the ureteral smooth muscles. Activation of the muscular wall biopotential is followed by 0.15-0.2 s contraction. The above effect was used by the authors in rehabilitation of 120 patients after ECIL. SMC and US were included into the physiotherapeutic complex. The above patients whose concrements after the fragmentation diminished to less than 7 cm in size were divided into 2 groups. Sixty patients of group 1 received spasmolytic drugs, sodium chloride or iodine-bromine baths and dynamic amplipulse therapy. Sixty patients of group 2 in addition to the above treatment were exposed to local vibration and US. All the patients were given antibacterial drugs. The percent of patients with complete urolith evacuation in group 1 amounted to 91.7%, with partial evacuation 8.3% (96.7 and 3.3% in group 2, respectively). Dynamic nephroscintigraphy demonstrated that after relevant physiotherapy renal function improved, leukocyte and red cell count in the urine and ferrum, alkaline phosphatase levels in the serum decreased.
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PMID:[Accelerated elimination of the stone fragments after extracorporeal shockwave lithotripsy]. 798 97

Body growth, blood chemistry, and long bone development of 10- to 16-day chick embryos (Gallus gallus) treated with aluminum (Al) citrate, sodium (Na) citrate, or sodium chloride (NaCl) were investigated. Two administration protocols were used. Acutely-treated embryos received 6.0 mumol Al citrate or Na citrate on day 8 of incubation. Chronically-treated embryos received a daily dose of 1.5 mumol Al citrate or Na citrate beginning on day 8 of incubation. For both protocols, Al citrate and Na citrate had no significant influence on viability or body weight. Al citrate-treated embryos had: (a) significantly shorter mean tibia lengths by day 16 of incubation, (b) a consistently lower ratio of tibia length: body weight on all days investigated, and (c) a persistent mid-diaphyseal malformation (angulation) of the femur and tibia. Spatially correlated with the malformation was a calcification defect detected by alizarin red S staining of intact tibias and the accumulation of aluminum as demonstrated by acid solochrome azurine staining of histological sections. Aluminum was localized at the mineralization front of the osteogenic collar surrounding the cartilage core of the tibia. Aluminum citrate or Na citrate had no significant effect on serum total calcium, inorganic phosphorus, total alkaline phosphatase activity, or creatinine, except for a transitory hypercalcemia (day 10) and phosphatemia (days 10 and 12) in Al citrate-treated embryos. The concomitant localization of Al and the early calcification defect in the region of tibial malformation implicate aluminum in the pathogenesis of the skeletal abnormality.
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PMID:Aluminum effects on blood chemistry and long bone development in the chick embryo. 799 19

Factor XIII A-chain-fibrin interactions regulate factor XIIIa formation and fibrin cross-linking. A microtiter plate assay was developed for studying these interactions. Microtiter plate wells were coated with fibrinogen and converted to fibrin by thrombin. After blocking the wells with bovine serum albumin, factor XIII A-chain was added and binding was monitored by incubating first with anti-factor XIII followed by anti-rabbit IgG-alkaline phosphatase. Enzymatic hydrolysis of p-nitrophenyl phosphate was quantitated by the absorbance at 405 nm. BInding was specific, sensitive, rapid, saturable, and reversible, requiring only nanograms of either factor XIII or fibrin. Binding was time- and concentration-dependent and independent of divalent cations. The bound material was identified as factor XIII A-chain by sodium dodecylsulfate-polyacrylamide gel electrophoresis and immunoblotting. Factor XIII binding was inhibited > 75% by 250 mM sodium chloride or 250 nM anti-factor XIII IgG. The method was also suitable for demonstrating binding using 0.8% plasma or with r-factor XIII expressed in Saccharomyces cerevisiae or Escherichia coli. This method is suitable for identifying the binding sites that are important for plasma factor XIII activation and factor XIIIa activity.
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PMID:A microtiter plate assay for factor XIII A-chain-fibrin interactions. 805 54


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