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Aspartate Aminotransferase

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101. Isolated elevated aspartate aminotransferase: a surprising outcome for clinicians. (Abstract)

Isolated elevated aspartate aminotransferase: a surprising outcome for clinicians. In this report a case of macro-aspartate aminotransferase in a 34-year-old pregnant woman is presented. Awareness of the existence of a macroenzyme is important because of their ability to cause diagnostic confusion, which leads to unnecessary investigations. Confirmation with a polyethylene glycol precipitation test is simple to perform and not expensive.

2012 Netherlands Journal of Medicine

102. The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues. Full Text available with Trip Pro

The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues. Carboxymethylated aspartate aminotransferase was digested with a proteinase claimed to be specific for lysine residues. Complete cleavage occurred at 12 of the 19 lysine residues in the protein, but at the remaining seven residues cleavage was either restricted or absent. In addition, cleavage was observed at three of the 26 arginine residues (...) . These results are discussed with reference to the amino acid residues adjacent to points of complete or restricted cleavage. The complete primary structure of aspartate aminotransferase, based on these and other studies, is given. Evidence for the assignment of some acid and amide side chains has been deposited as Supplementary Publication SUP 50050 (11 pp.) at the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated

1975 Biochemical Journal

103. Purification and some properties of cytoplasmic aspartate aminotransferase from sheep liver Full Text available with Trip Pro

Purification and some properties of cytoplasmic aspartate aminotransferase from sheep liver 1. A procedure for the purification of the cytoplasmic isoenzyme of aspartate aminotransferase from sheep liver is described. 2. The purified isoenzyme shows a single component in the ultracentrifuge at pH7.6 and forms a single protein band on agar-gel electrophoresis at pH6.3 or 8.6, as well as when stained for protein or activity after polyacrylamide-gel or cellulose acetate electrophoresis at pH8.8. 3

1973 Biochemical Journal

104. The sequences of the coenzyme-binding peptide in the cytoplasmic and the mitochondrial aspartate aminotransferases from sheep liver. Full Text available with Trip Pro

The sequences of the coenzyme-binding peptide in the cytoplasmic and the mitochondrial aspartate aminotransferases from sheep liver. The sequences of the coenzyme-binding peptide of both cytoplasmic and mitochondrial aspartate aminotransferases from sheep liver were determined. The holoenzymes were treated with NaBH4 and digested with chymotrypsin; peptides containing bound pyridoxal phosphate were then isolated. One phosphopyridoxyl peptide was obtained from sheep liver cytoplasmic aspartate (...) aminotransferase. Its sequence was Ser-Ne-(phosphopyridoxyl)-Lys-Asn-Phe. This sequence is identical with that reported for the homologous peptide from pig heart cytoplasmic aspartate aminotransferase. Two phosphopyridoxyl peptides with different RF values were isolated from the sheep liver mitochondrial isoenzyme. They had the same N-terminal amino acid and similar amino acid composition. The mitochondrial phosphopyridoxyl peptide of highest yield and purity had the sequence Ala-Ne-(phosphopyridoxyl)-Lys-Asx

1975 Biochemical Journal

105. Studies on the changes in protein fluorescence and enzymic activity of aspartate aminotransferase on binding of pyridoxal 5′-phosphate Full Text available with Trip Pro

Studies on the changes in protein fluorescence and enzymic activity of aspartate aminotransferase on binding of pyridoxal 5′-phosphate 1. The alpha and beta subforms of aspartate aminotransferase were purified from pig heart. 2. The alpha subform contained 2mol of pyridoxal 5'-phosphate. The apo-(alpha subform) could be fully reactived by combination with 2mol of cofactor. 3. The protein fluorescence of the apo-(alpha subform) decreased non-linearly with increase in enzyme activity

1974 Biochemical Journal

106. The anomalous kinetics of coupled aspartate aminotransferase and malate dehydrogenase. Evidence for compartmentation of oxaloacetate. Full Text available with Trip Pro

The anomalous kinetics of coupled aspartate aminotransferase and malate dehydrogenase. Evidence for compartmentation of oxaloacetate. Cytoplasmic aspartate aminotransferase and malate dehydrogenase were purified from pig heart. Kinetic parameters were determined for the separate reaction catalysed by each enzyme and used to predict the course of the coupled reaction: (see article). Although a lag phase should have been easily seen, none was detected. The same coupled reaction was also carried (...) out by using radioactive aspartate in the presence of unlabelled oxaloacetate. The reaction was quenched with HClO4 after 70 ms and the specific radioactivity of the malate produced in this system was found to be essentially the same as that of the original aspartate. These results show that oxaloacetate produced by the aspartate aminotransferase is converted into malate by malate dehydrogenase before it equilibrates with the pool of unlabelled oxaloacetate and are consistent with a proposal

1976 Biochemical Journal

107. Genetic Analysis of Aspartate Aminotransferase Isozymes from Hybrids between DROSOPHILA MELANOGASTER and DROSOPHILA SIMULANS and Mutagen-Induced Isozyme Variants Full Text available with Trip Pro

Genetic Analysis of Aspartate Aminotransferase Isozymes from Hybrids between DROSOPHILA MELANOGASTER and DROSOPHILA SIMULANS and Mutagen-Induced Isozyme Variants The aspartate aminotransferases (designated GOT1 and GOT2) are two enzymes of Drosophila melanogaster for which naturally occurring electrophoretic variants were not found. There is an electrophoretic difference between D. melanogaster and D. simulans. Since the F1 hybrid offspring of these species are sterile, a genetic analysis

1976 Genetics

108. The interaction of aliphatic and aromatic dicarboxylic acids with aspartate aminotransferase. Full Text available with Trip Pro

The interaction of aliphatic and aromatic dicarboxylic acids with aspartate aminotransferase. 4672664 1972 11 29 2018 11 13 0264-6021 126 3 1972 Feb The Biochemical journal Biochem. J. The interaction of aliphatic and aromatic dicarboxylic acids with aspartate aminotransferase. 20P-21P Harris H H Kalogerakos T T Evangelopoulos A E AE Bayley P M PM eng Journal Article England Biochem J 2984726R 0264-6021 0 Dicarboxylic Acids EC 2.6.1.1 Aspartate Aminotransferases IM Animals Aspartate (...) Aminotransferases Binding Sites Dicarboxylic Acids Hydrogen-Ion Concentration Myocardium enzymology Spectrum Analysis Swine 1972 2 1 1972 2 1 0 1 1972 2 1 0 0 ppublish 4672664 PMC1178470 J Biol Chem. 1966 Jun 25;241(12):2845-54 5912360 J Biol Chem. 1967 May 25;242(10):2397-409 4961055 J Biol Chem. 1970 Jan 25;245(2):262-9 4312670 J Biol Chem. 1962 Jul;237:2109-22 13925259 J Biol Chem. 1965 Jul;240:2907-13 14342314

1972 Biochemical Journal

109. Nonidentity of the Aspartate and the Aromatic Aminotransferase Components of Transaminase A in Escherichia coli Full Text available with Trip Pro

Nonidentity of the Aspartate and the Aromatic Aminotransferase Components of Transaminase A in Escherichia coli Tyrosine, added to the growth medium of a strain of Escherichia coli K-12 lacking transaminase B, repressed the tyrosine, phenylalanine, and tryptophan aminotransferase activities while leaving the aspartate aminotransferase activity unchanged. This suggested that the aspartate and the aromatic aminotransferase activities, previously believed to reside in the same protein, viz (...) . transaminase A, are actually nonidentical. Further experiments showed that, upon incubation at 55 C, the aspartate aminotransferase of crude extracts was almost completely stable, whereas the tyrosine and phenylalanine activities were rapidly inactivated. Apoenzyme formation was faster, and apoenzyme degradation proceeded more slowly with aspartate aminotransferase than with tyrosine aminotransferase. Electrophoresis in polyacrylamide gels separated the aminotransferases. A more rapidly moving band

1972 Journal of bacteriology

110. The nature of the multiple forms of cytoplasmic aspartate aminotransferase from pig and sheep heart Full Text available with Trip Pro

The nature of the multiple forms of cytoplasmic aspartate aminotransferase from pig and sheep heart Starch-gel electrophoresis of sheep heart aspartate aminotransferase was carried out over the range pH7.0-8.5. The enzyme separates into three subforms in the same way as the pig heart enzyme. As the pH was increased the distance migrated by each subform increased by the same amount, so that they remained the same distance apart. Titration of the enzyme over the appropriate pH range was used

1974 Biochemical Journal

111. Effect of pH, ionic strength and univalent inorganic ions on the reconstitution of aspartate aminotransferase Full Text available with Trip Pro

Effect of pH, ionic strength and univalent inorganic ions on the reconstitution of aspartate aminotransferase 1. The effect of pH change on the reconstitution of aspartate aminotransferase (EC 2.6.1.1), i.e. the reactivation of the apoenzyme with coenzyme (pyridoxal phosphate and pyridoxamine phosphate), was studied in the pH range 4.2-8.9 by using three buffer systems at concentrations ranging from 0.025 to 0.1m. 2. Although the profile of the reconstitution rate-pH curve in the range pH5.2

1974 Biochemical Journal

112. EFFECTS OF FIXATION AND SUBSTRATE PROTECTION ON THE ISOENZYMES OF ASPARTATE AMINOTRANSFERASE STUDIED IN A QUANTITATIVE CYTOCHEMICAL MODEL SYSTEM Full Text available with Trip Pro

EFFECTS OF FIXATION AND SUBSTRATE PROTECTION ON THE ISOENZYMES OF ASPARTATE AMINOTRANSFERASE STUDIED IN A QUANTITATIVE CYTOCHEMICAL MODEL SYSTEM The cytochemical technique of Lee and Torack for the demonstration of aspartate aminotransferase activity was tested on a model system consisting of either total liver homogenate or the mitochondrial or soluble cytoplasmic fraction, incorporated in polyacrylamide film. After incubation of portions of film in a medium of alpha-ketoglutarate, L-aspartate (...) , and lead nitrate, the lead oxaloacetate formed was converted to lead sulfide. The absorbance determined at 520 nm in a film spectrophotometer and expressed in terms of unit weight of film provided a measure of the contained enzymatic activity, and was directly proportional to the concentration of chemically determined oxaloacetate in the film. Both mitochondrial and "soluble" isozymes of aspartate aminotransferase reacted with the cytochemical media to a quantitatively similar degree, but were

1970 The Journal of cell biology

113. THE ULTRASTRUCTURAL LOCALIZATION OF THE ISOZYMES OF ASPARTATE AMINOTRANSFERASE IN MURINE TISSUES Full Text available with Trip Pro

THE ULTRASTRUCTURAL LOCALIZATION OF THE ISOZYMES OF ASPARTATE AMINOTRANSFERASE IN MURINE TISSUES Two isozymes of aspartate aminotransferase have been demonstrated biochemically. One isozyme is found in the mitochondrial fraction of the cytoplasm, the other ("soluble") in the supernatant. Both isozymes can be demonstrated by the cytochemical technique of Lee and Torack, as reported in the preceding report. Aldehyde fixation rapidly inactivates both isozymes, especially the soluble one (...) . Inactivation can be delayed by addition of ketoglutarate to the fixative. The ketoglutarate probably competes with the fixative for the active site of the enzyme, thus protecting that region of the molecule. This enables adequate tissue preservation with enough remaining enzymatic activity to be demonstrated by the precipitation of oxaloacetate as the lead salt from a medium containing alpha-ketoglutaric acid aspartic acid, and lead nitrate. Electron-opaque material was found not only in mitochondria

1970 The Journal of cell biology

114. Selective permeability of rat liver mitochondria to purified aspartate aminotransferases in vitro. Full Text available with Trip Pro

Selective permeability of rat liver mitochondria to purified aspartate aminotransferases in vitro. 1. A method was devised to allow determination of intramitochondrial aspartate amino-transferase activity in suspensions of intact mitochondria. 2. Addition of purified rat liver mitochondrial aspartate aminotransferase to suspensions of rat liver mitochondria caused an apparent increase in the intramitochondrial enzyme activity. No increase was observed when the mitochondria were preincubated (...) with the purified cytoplasmic isoenzyme. 3. These results suggest that mitochondrial aspartate aminotransferase, but not the cytoplasmic isoenzyme, is able to pass from solution into the matrix of intact rat liver mitochondria in vitro. 4. This system may provide a model for studies of the little-understood processes by which cytoplasmically synthesized components are incorporated into mitochondria in vivo.

1977 Biochemical Journal

115. Interaction of aspartate aminotransferase with mercurochrome. Relationship of an exposed thiol group of the enzyme to the active centre. Full Text available with Trip Pro

Interaction of aspartate aminotransferase with mercurochrome. Relationship of an exposed thiol group of the enzyme to the active centre. Mercurochrome strongly inhibits aspartate transaminase and 2,3-dicarboxyethylated aspartate transaminase. The native enzyme exhibits a biphasic time-course of inactivation by mercurochrome with second-order rate constants 1.62 x 10(4) M-1 - min-1 and 2.15 x 10(3) M-1 - min-1, whereas the modified enzyme is inactivated more slowly (second-order rate constant

1977 Biochemical Journal

116. Syncatalytic conformational changes in aspartate aminotransferase determined by hydrogen-deuterium exchange. Full Text available with Trip Pro

Syncatalytic conformational changes in aspartate aminotransferase determined by hydrogen-deuterium exchange. Catalysis-linked conformational transitions of aspartate aminotransferase (cytosolic isoenzyme from pig heart; L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) have been probed by infrared spectrophotometric measurement of hydrogen-deuterium exchange. In the unliganded pyridoxal form of the enzyme at pH 6.0 and 20 degrees, 43% of the total 411 peptide hydrogens per subunit

1978 Proceedings of the National Academy of Sciences of the United States of America

117. The binding of 8-anilinonaphthalene-1-sulphonate to cytoplasmic aspartate aminotransferase from pig heart. Full Text available with Trip Pro

The binding of 8-anilinonaphthalene-1-sulphonate to cytoplasmic aspartate aminotransferase from pig heart. Anilinonaphthalenesulphonate binds to cytoplasmic aspartate aminotransferase with high affinity (Kd about 10 muM) and with a stoicheiometry of one molecule per dimer. It is not displaced by aliphatic or aromatic dicarboxylate substrate analogues. The enzyme is believed to be a symmetrical dimer with identical subunits; it can evidently function asymmetrically in binding

1975 Biochemical Journal

118. Some kinetic and other properties of the isoenzymes of aspartate aminotransferase isolated from sheep liver. Full Text available with Trip Pro

Some kinetic and other properties of the isoenzymes of aspartate aminotransferase isolated from sheep liver. A method for the purification of mitochondrial isoenzyme of sheep liver aspartate aminotransferase (EC 2.6.1.1) is described. The final preparation is homogeneous by ultracentrifuge analyses and polyacrylamide-gel electrophoresis and has a high specific activity (182 units/mg). The molecular weight determined by sedimentation equilibrium is 87,100 +/- 680. The amino acid composition (...) is presented; it is similar to that of other mitochondrial isoenzymes, but with a higher content of tyrosine and threonine. Subforms have been detected. On isoelectric focusing a broad band was obtained, with pI 9.14. The properties of the mitochondrial aspartate aminotransferase are compared with those of the cytoplasmic isoenzyme. The Km for L-aspartate and 2-oxoglutarate for the cytoplasmic enzyme were 2.96 +/- 0.20 mM and 0.093 +/- 0.010 mM respectively; the corresponding values for the mitochondrial

1979 Biochemical Journal

119. The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastase Full Text available with Trip Pro

The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastase Peptides produced by thermolytic digestion of aminoethylated aspartate aminotransferase and of the oxidized enzyme were isolated and their amino acid sequences determined. Digestion by elastase of the carboxymethylated enzyme gave peptides representing approximately 40% of the primary structure. Fragments from these digests overlapped with previously

1973 Biochemical Journal

120. The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with pepsin and trypsin Full Text available with Trip Pro

The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with pepsin and trypsin Peptides obtained by tryptic digestion of carboxymethylated and maleylated aspartate aminotransferase and of the aminoethylated enzyme were isolated and the complete amino acid sequences of most of them were determined. Digestion of the carboxymethylated protein with pepsin produced a complex mixture of peptides that allowed some overlapping of the tryptic

1972 Biochemical Journal

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