Phosphatase acid alkaline

Phosphatases Acid phosphatase Alkaline phosphatase ATPase (sarcoplasmic reticulum) ATPase (mitochondrial)... 

Blood Alkaline phosphatase (bone-specific) Osteocalcin Procollagen type I carboxy-terminal propeptide (PICP) Procollagen type I amino-terminal propeptide (PINP) Procollagen type III amino-terminal propeptide (PIIINP) Blood Acid phosphatase (acid-resistant) Type I collagen carboxy-terminal telopeptide (ICTP) Urine Calcium Hydroxyproline Cross-linked peptides (pyridinium and deoxypyridinoline)... 

The results of that experiment allow one to synthesize a-D-ribose-l-[l80U]-phosphate which can be employed to determine the position of bond cleavage by other enzymes whose role is transfer of phosphate (Pj) to water or to another acceptor. We report results on a. the position of bond cleavage in R-l-P by PNP from human erythrocytes and E. coli as well as by alkaline phosphatase, acid phosphatase, formic acid andb. the position of bond making in ribose-5-phosphate by phosphoglucomutase. The earlier experiment from this laboratory employed the equilibration ... 

Alkaline phosphatase, acid phosphatase, 5 -nucleotidase, monoacyl hydrolase, ribonuclease, type 1 phosphodiesterase, adenosine triphosphatase, adenyl cyclase, glycosyl transferase, esterases and disaccharidase have been biochemically or cytochemically demonstrated in the tegument of various cestodes (152, 210, 250, 374, 491, 620, 624-626, 651, 718, 763, 776, 898). Several of these enzymes - phosphatases, 5 -nucleotidase and phosphodiesterase - probably have a digestive and/or absorptive function but the role of the others is uncertain. 

Amino benzyl phosphonic acid Alkaline and acid phosphatases... 

Heterogeneous phosphorylation is often a problem when kinases are expressed in insect cells. Multiple approaches have been used to solve this problem. Proteins have been completely dephosphorylated by incubation with A protein phosphatase or alkaline phosphatase [38, 39, 56]. Ion exchange and isoelectric focusing chromatography have been used to separate proteins with multiple phosphorylation states. An y-aminophenyl ATP-sepharose column was used to separate different phosphory-lated states of human c-Src [34]. Alternatively, serine/threonine or tyrosine phosphorylation sites can be mutated to alanine or phenylalanine, respectively [42]. For tyrosine kinases with multiple autophosphorylation sites, the active site aspartic acid can be mutated to an asparagine, creating a kinase dead mutant [57]. 

In general there are three phosphatase families alkaline, acid, and protein phosphatases. Alkaline phosphatases are typically dimers that contain three metal ions per subunit and have a pH optimum pH above 8. Acid phosphatases exhibit an optimum pH<7 and are usually divided into three classes low molecular weight acid phosphatases (<20 kDa), high molecular weight acid phosphatases (50-60 kDa), and purple acid phosphatases (which contain an Fe-Fe or Fe-Zn center at the active site). Phosphatases specific for I-l-P appear to be most similar (in kinetic characteristics but not in mechanism) to the alkaline phosphatases, but their structures define a superfamily that also includes inositol polyphosphate 1-phosphatase, fructose 1, 6-bisphosphatase, and Hal2. The members of this superfamily share a common structural core of 5 a-helices and 11 (3-strands. Many are Li+-sensitive (York et al., 1995), and more recent structures of archaeal IMPase proteins suggest the Li+ -sensitivity is related to the disposition of a flexible loop near the active site (Stieglitz et al., 2002). 

The pharmacological effects and therapeutic uses of SAMe in hepatology are discussed in a detailed review. (169) The impressive outcome of various experiments led to numerous clinical studies, which, however, also included negative results. (165, 169, 174-176) On the whole, there was a significant decrease in bilirubin, bile acids, alkaline phosphatase and transaminases. Pruritus, a frequent symptom in cholestasis, also showed regression. 

Another important hydrolytic enzyme of the gut is acid phosphatase Like enterokinasc, it is bound to the enierocyte facing the lumen and is present in the duodenum, jejunum, and ileum. Alkaline phosphatase, a zinc metalloenzyme, also occurs in the gut. Acid phosphatase and alkaline phosphatase catalyze the removal of phosphate groups from a wide variety of compounds in foods, for example, sugar phosphates, triose phosphates, nucleotides such as AMP, ADP, and ATP, pyrophosphate, and phosphorylaled amino adds, A number of sugar and triose phosphates are described in the section on glycolysis in Chapter 4,... 

D-Glucosamine 6-phosphate is hydrolyzed by the D-glucose-6-phosphatase of rat-liver mitochondria. The rate of this hydrolysis is about 8 % of that of D-glucose 6-phosphate hydrolysis. A phosphatase which preferentially catalyzes the hydrolysis of D-glucosamine 6-phosphate has been prepared from Neurospora crassa. This enzyme is not stimulated by magnesium ions and has an optimum activity between pH 6 and 7.5. It appears to be distinct from acid, alkaline, and other specific phosphatases. 

Found in some Alkaline phosphatase, acid phosphatase. 

The co-administration of M. oleifera seed powder with arsenic protects animals from arsenic induced oxidative stress and reduce body arsenic burden (49). Exposure of rats to arsenie (2.5 mg/kg, intraperitoneally for 6 weeks) increases the levels of tissue reaetive oxygen species (ROS), metallothionein (MT) and thiobarbitnrie aeid reaetive substance (TEARS) and is accompanied by a decrease in the aetivities in the antioxidant enzymes such as superoxide dismutase (SOD), eatalase and glutathione peroxidase (GPx). Also, Arsenic exposed mice exhibits hver injury as reflected by reduced acid phosphatase (AGP), alkaline phosphatase (ALP) and aspartate aminotransferase (AST) activities and altered heme synthesis pathway as shown by inhibited blood 8-aminolevulinic acid dehydratase (5-ALAD) activity. Co-administration of M. oleifera seed powder (250 and 500 mg/kg, orally) with arsenie significantly increases the activities of SOD, catalase, GPx with elevation in redueed GSH level in tissues (liver, kidney and brain). These ehanges are accompanied by approximately 57%, 64% and 17% decrease in blood ROS, liver metallothionein (MT) and lipid peroxidation respectively in animal eo-administered with M. oleifera and arsenic. There is a reduced uptake of arsenie in soft tissues (55% in blood, 65% in liver, 54% in kidneys and 34% in brain) following eo-administration of M. oleifera seed powder (particularly at the dose of 500 mg/kg). This points to the fact that administration of M. oleifera seed powder could be beneficial during chelation therapy with a thiol chelator (26). 

Antibody-masking enzyme tag immunoassay Adenosine 5 -monophosphate S-Acetylmercaptosuccinic anhydride Alkaline phosphatase anti-alkaline phosphatase (enzyme-antibody) complex Alkaline phosphatase 5-Aminosalicylic acid Adenosine 5 -triphosphate Aa-Benzoyl-L-arginine ethyl ester (-f-)-Biotin bromoacetyl hydrazide (-b)-Biotin Y-aminocaproic acid A-hydroxy-succinimide ester Bis-diazotized benzidine -Galactosidase (-I- )-Biotin hydrazide (-I- )-Biotin-A-hydroxysuccinimide ester (-I-)-Biotin p-nitrophenyl ester Bridged avidin-biotin (method)... 

The activity of glycosyltransferases can also be monitored throughout the reaction comse by removing a small aliquot from the reaction, followed by dilution and assay of activity by one of the standard assays with defined substrates in Table 1. It is desirable to monitor the pH of the reaction closely, especially when the concentration of the substrate is relatively high compared to molarity of the buffer. The pH of glycosyltransferase reactions drops as reactions proceed as a result of the production of phosphoric acid by alkaline phosphatase. Acidic pH values can inactivate glycosyltransferases and substrates, and decrease the efficiency of alkaline phosphatase. 

G12. Gonzalez-Oddone, M. V., BiUrubin, bromsulphthalein, bile acids, alkaline phosphatase and cholesterol of thoracic duct lymph in experimental regurgitation jaundice. Proc. Soc. Exptl. Biol. Med. 63, 144-147 (1946). 

Two enzymatic systems, i.e., calpain and cathepsin influence tenderization of meat. The activity of calpain reduces under high pressure. The activity of p-calpain is also reduced during ageing (Ouali, 1990). Qin et al. (2001) showed that high-pressure treatment (100-300 MPa, 10 min) of beef resulted in a decrease in the total calpain activity however, the acid phosphatase and alkaline phosphatase activities were not significantly reduced. Homma et al. (1995) found that the total activity of calpain in pressurized muscle increased due to a reduction in the level of calpastatin because of its pressure sensitivity this in turn resulted in meat tenderization. 

Husain et al. studied the effects of CR and CN aerosols on clinical chemistry parameters (e.g., plasma glutamic-oxaloacetic tansaminase (GOT), plasma glutamic-pyruvic transaminase (GPT), acid phosphatase, and alkaline phosphatase). Rats were exposed via inhalation to aerosols of CR or CN. Animals exposed to CR aerosol exhibited no significant changes in plasma GOT and GPT activities or in acid and alkaline phosphatase activities. In contrast, CN-exposed animals manifested significant increases in GOT, GPT, acid phosphatase, and alkaline phosphatase activities. The conclusion drawn from the study was that exposure to CN aerosol could lead to tissue damage. 

Pancreatic ribonuclease is markedly inhibited by heparinoids but not by mucopolysaccharides, with sulphated polyvinyl alcohol >sulphated corn amylosOsulphated cellulose > sulphated corn amylopectin> sulphated dextran, sulphated pectic acid, polyvinyl sulphonate with 2 T 7 per cent sulphur>sulphated nitro chitin, sulphated nitro chitosan and heparin . Single injections of heparin in mice result in significant inhibition of the acid alkaline ribonuclease of the liver after the injection. This probably explains the accumulation of ribonucleic acid in tissue culture cells in the presence of heparin. Heparin also inhibits rat acid phosphatase, glucuronidase , catalase , fumarase and elastase. 

Depending on pH, phosphomonoesterases have been grouped into acid phosphatase and alkaline phosphatase. Optimum pH range of 4-6 for acid phosphatase and S.3-9.5 for alkaline phosphatase... 

Alkaline phosphatase acid phosphatase acetylcholinesterase Glycerol 3-P oxidase Alcohol oxidase Sarcosine oxidase Urease... 

Calyctiins, Strongly antitumor active metabolites from the Japanese marine sponge Discodermia calyx. Phosphatases 1 and 2A have been identified as the molecular sites of action. IC50O.5-2 nM(PPl) 0.1 -1 nM (PP2A). With regard to PPl C. A is about 30-200 times more effective than okadaic acid. Acidic, alkaline, and protein-tyrosine phosphatases are not affected. C. is cell permeable and can be used to study... 

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