Amino acid alkaline phosphatase

Alcohol dehydrogenase, 178 Alkaline error, 149 Alkaline phosphatase, 185 Alkanethiols, 46, 123 Alkoxide precursor, 120 Amino acids, 92, 187 Ammonium sensor, 181, 182 Amperometric sensors, 172 Aniline, 35, 39... 

F (increases in alkaline phosphatase(48%), glutamate oxaloacetate transaminase (82%) glutamate pyruvate transaminase (55%), isocitrate dehydrogenase (65%), cholesterol (27%-35%), and soluble proteins (35%) decreases in free amino acids (34-40%) and glucose (41-51%) vacuolization fatty infiltration)... 

Amifostine is hydrolyzed rapidly to 2-[(3-aminopropyl)amino]ethane-thiol (9.64) at the acidic pH of the stomach, and by alkaline phosphatases in various tissues. After intravenous administration to cancer patients, the plasma half-lives were found to be in the order of minutes. This is highly relevant, since most or all pharmacological effects of amifostine can be ascribed to its thiol metabolite. 

Brydon and Roberts- added hemolyzed blood to unhemolyzed plasma, analyzed the specimens for a variety of constituents and then compared the values with those in the unhemolyzed plasma (B28). The following procedures were considered unaffected by hemolysis (up to 1 g/100 ml hemoglobin) urea (diacetyl monoxime) carbon dioxide content (phe-nolphthalein complex) iron binding capacity cholesterol (ferric chloride) creatinine (alkaline picrate) uric acid (phosphotungstate reduction) alkaline phosphatase (4-nitrophenyl phosphate) 5 -nucleotidase (adenosine monophosphate-nickel) and tartrate-labile acid phosphatase (phenyl phosphate). In Table 2 are shown those assays where increases were observed. The hemolysis used in these studies was equivalent to that produced by the breakdown of about 15 X 10 erythrocytes. In the bromocresol green albumin method it has been reported that for every 100 mg of hemoglobin/100 ml serum, the apparent albumin concentration is increased by 100 mg/100 ml (D12). Hemolysis releases some amino acids, such as histidine, into the plasma (Alb). 

Alkaline hydrolysis, see Saponification Alkaline phosphatase (AP), in immunoblotting, 207-217 Amido black, staining of proteins blots, 199-200 Amino acids... 

The amino acid composition of alkaline phosphatase of E. coli is given in Table II (41, 45, 45, 47) The values from Lazdunski and Lazdunski... 

The amino acid sequence around the serine that is phosphorylated in the presence of inorganic phosphate at low pH can be seen in Table III (55-57). The sequence of Schwartz et al. (55) accounted for 56% of the peptides that contained 32P (20% or more of the peptides were excluded as extreme fractions when the peaks were pooled). The sequence, as far as it is known, is the same for alkaline phosphatase from a mammalian source (58). It is interesting to note, as pointed out by Boyer and others (59-64), that many hydrolytic enzymes with a serine residue at their active site have the same general sequence, i.e., Asp (Glu)-Ser-Ala (Gly). 

Schlesinger and Anderson (44) separated the isozymes on starch-gel and DEAE-cellulose at various times after 14C-amino acids were added to a culture of E. coli synthesizing alkaline phosphatase. They found that initially most of the counts appeared in isozyme I, but later they appeared mainly in isozymes II and III. In another experiment where only enough radioactive amino acid was added to allow for 5 min of synthesis of radioactive protein, they found that the label is initially found in isozymes I and II and later in isozymes II and III. These experiments establish that the monomers of isozyme I are precursors for isozymes II and III. 

Amino Acid Composition of Human Placental Alkaline Phosphatase... 

This feature has been extensively investigated by Engstrom (20, 71, 88, 168, 169 see also Sections I,A and II,B) whose results may be summarized as follows (1) incubation of alkaline phosphatase with 32P-Pi at pH 4—6 and 0°, followed by acid inactivation, leads to the appearance of the label in the enzyme protein (2) after acid hydrolysis the only labeled amino acid found is phosphoserine (3) one mole of Pi is incorporated per mole of enzyme (4) the presence of Zn2+ in the enzyme is essential for phosphorylation (5) bound Pi can be displaced by addition of glucose 6-phosphate to the phosphorylation medium and (6) very little phosphoryl enzyme is formed under alkaline conditions. 

On the other hand, alkaline phosphatase may have two equivalent active sites which are coupled so that, normally, only one can operate at a time. This seems an attractive alternative for an enzyme consisting of two identical subunits. In a preliminary paper, Lazdunski et al. (125) report the covalent incorporation of two phosphates into the zinc enzyme as well as the cobalt enzyme, at >H<4. At these low pH values, the free enzyme generally loses its metal ions and dissociates into monomeres (109). However, if these results are corroborated after the performance of proper controls, and if both phosphates are linked to specific amino acid residues in the enzyme, conditions may have been found for the uncoupling of active sites in alkaline phosphatase. 

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)... 

Alkaline phosphatase 515, 535-538, 611, 616, 620, 627, 629, 916, 918, e252, e257-e258, e261 Alkanethiol 193, 196, 203, 245 Alkanethiolate layer 922 Alkylthiols el05, el09 Alpha-1-fetoprotein 513 Amino acid 189, 191-192, 256, 508, 513, 531, 536... 

Enzymes are biocatalysts constructed of a folded chain of amino acids. They may be used under mild conditions for specific and selective reactions. While many enzymes have been found to be catalytically active in both aqueous and organic solutions, it was not until quite recently that enzymes were used to catalyze reactions in carbon dioxide when Randolph et al. (1985) performed the enzyme-catalyzed hydrolysis of disodium p-nitrophenol using alkaline phosphatase and Hammond et al. (1985) used polyphenol oxidase to catalyze the oxidation of p-cresol and p-chlorophenol. Since that time, more than 80 papers have been published concerning reactions in this medium. Enzymes can be 10-15 times more active in carbon dioxide than in organic solvents (Mori and Okahata, 1998). Reactions include hydrolysis, esterification, transesterification, and oxidation. Reactor configurations for these reactions were batch, semibatch, and continuous. 

Studies in animals suggest that chlorobenzene may also cause injury to the liver. In rats, alkaline phosphatase, SGOT, and delta-amino levulinic acid levels were increased as were liver protoporphyrin and uroporphyrin. Data suggest that the kidneys may be affected following exposure to chlorobenzene as polyuria was noted in rats at high dose levels. Since other chemicals may produce similar effects, these are not specific indicators of chlorobenzene exposure. 

The enzymes used to generate reactive quinone methides often undergo inactivation by addition of this electrophile to essential nucleophilic amino acid side chains of the protein catalyst. This is a type of suicide enzyme inhibition.80 This was observed for the acid phosphatase and ribonuclease catalysts used to generate 43.76 79 Alkaline phosphatase has been used to remove the phosphate protecting group from a derivative of an o-difluoromethyl phenyl phosphate that was covalently attached to a solid support. Breakdown of the immobilized 4-hydroxybenzyl difluoride gives an immobilized quinone methide that, in principle, will react irreversibly with proteins and lead to their attachment to the solid support.81... 

Mocarelli et al. (1986) conducted a 6-year study on clinical laboratory parameters of children exposed to 2,3,7,8-TCDD following the Seveso accident. ALT, aspartate aminotransferase (AST), GGT, alkaline phosphatase, cholesterol, and triglycerides in plasma and delta amino levulinic acid in urine were monitored yearly in exposed and control groups beginning in June, 1977, approximately 1 year after the incident. The children were 6-10 years old at the time of the accident 69, 528, and 874 resided in the A, B, and R zones, respectively. Chloracne was seen in 19, 0.7, and 4.6%, of the children in areas A, B, and R, respectively. Blood samples were drawn from 69, 83, and 221 children in areas A, B, and R,... 

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