How to Trip Rapid Review

Step 1: Select articles relevant to your search (remember the system is only optimised for single intervention studies)

Step 2: press

Step 3: review the result, and maybe amend the or if you know better! If we're unsure of the overall sentiment of the trial we will display the conclusion under the article title. We then require you to tell us what the correct sentiment is.

16,853 results for

Aspartate Aminotransferase

by
...
Latest & greatest
Alerts

Export results

Use check boxes to select individual results below

SmartSearch available

Trip's SmartSearch engine has discovered connected searches & results. Click to show

121. Evidence for the participation of aspartate aminotransferase in hepatic glucose synthesis in the suckling newborn rat. (Full text)

Evidence for the participation of aspartate aminotransferase in hepatic glucose synthesis in the suckling newborn rat. Inhibition of liver aspartate aminotransferase by L-2-amino-4-methoxy-trans-3-butenoic acid in the suckling newborn rat causes a decrease in all gluconeogenic precursors from phosphoenolpyruvate to glucose and an accumulation of lactate but not of pyruvate. This suggests that the aspartate shuttle is operative and confirms the quantitative importance of lactate

1978 Biochemical Journal

122. Some kinetic and other properties of the isoenzymes of aspartate aminotransferase isolated from sheep liver. (Full text)

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

123. Generation of aspartate aminotransferase multiple forms by deamidation. (Full text)

Generation of aspartate aminotransferase multiple forms by deamidation. The development of aspartate aminotransferase subforms in vitro was followed by densitometry after thin-film isoelectric focusing. At the same time ammonia production was measured. Each reaction can be expressed in terms of a first-order process in which 2 mol of glutamine or asparagine/mol of dimer are deamidated with a half time of 22 days. The more negatively charged subforms developed in vitro were almost fully active

1979 Biochemical Journal

124. The binding of pyridoxal 5-phosphate to aspartate aminotransferase of pig heart (Full text)

The binding of pyridoxal 5-phosphate to aspartate aminotransferase of pig heart 13976516 1998 11 01 2018 12 01 0264-6021 88 1963 Jul The Biochemical journal Biochem. J. The binding of pyridoxal 5-phosphate to aspartate aminotransferase of pig heart. 172-5 SCARDI V V SCOTTO P P IACCARINO M M SCARANO E E eng Journal Article England Biochem J 2984726R 0264-6021 5V5IOJ8338 Pyridoxal Phosphate EC 2.6.1.1 Aspartate Aminotransferases OM Animals Aspartate Aminotransferases Heart Humans Myocardium (...) Pyridoxal Phosphate Sus scrofa Swine ASPARTATE AMINOTRANSFERASE MYOCARDIUM PYRIDOXAL PHOSPHATE 1963 7 1 1963 7 1 0 1 1963 7 1 0 0 ppublish 13976516 PMC1203869 J Biol Chem. 1951 Nov;193(1):45-52 14907688 J Biol Chem. 1959 Jan;234(1):51-7 13610891 Boll Soc Ital Biol Sper. 1960 Dec 31;36:1719-22 13747074 J Biol Chem. 1960 Mar;235:620-4 14407079 Biochem J. 1962 May;83:413-6 14497811

1963 Biochemical Journal

125. Aspartate aminotransferase. The effects of ionic concentration on kinetic constants of both isoenzymes (Full text)

Aspartate aminotransferase. The effects of ionic concentration on kinetic constants of both isoenzymes 1. The Michaelis constants for both isoenzymes for both substrates depend strongly on ionic concentration, being approximately proportional to phosphate concentration over considerable ranges. This is probably an effect of anions only. 2. In the absence of added salt, K(m) (2-oxoglutarate) (anionic isoenzyme) is so small as to be indeterminate. 3. K(m) (l-aspartate) (anionic isoenzyme) passes

1968 Biochemical Journal

126. The interaction between α2-macroglobulin and cationic aspartate aminotransferase (Full text)

The interaction between α2-macroglobulin and cationic aspartate aminotransferase On starch-gel or polyacrylamide-gel electrophoresis of human serum, a supernumerary zone of aspartate aminotransferase activity may be demonstrated, migrating with the slow alpha(2) protein zone. This appearance is due only to cationic aspartate aminotransferase, bound by alpha(2)-macroglobulin. The binding is strongly potentiated by dilute borate buffers.

1969 Biochemical Journal

127. Dissociation of the prosthetic group of aspartate aminotransferase. (Full text)

Dissociation of the prosthetic group of aspartate aminotransferase. 5726192 1969 02 04 2018 11 13 0264-6021 110 2 1968 Nov The Biochemical journal Biochem. J. Dissociation of the prosthetic group of aspartate aminotransferase. 18P-19P Dixon H B HB Severin E S ES eng Journal Article England Biochem J 2984726R 0264-6021 0 Glutamates EC 2.6.1.1 Aspartate Aminotransferases IM Animals Aspartate Aminotransferases Chemical Phenomena Chemistry Chromatography, Gel Glutamates Swine 1968 11 1 1968 11 1 0

1968 Biochemical Journal

128. Regeneration of aspartate aminotransferase from its apoenzyme. (Full text)

Regeneration of aspartate aminotransferase from its apoenzyme. 5726194 1969 02 04 2018 11 13 0264-6021 110 2 1968 Nov The Biochemical journal Biochem. J. Regeneration of aspartate aminotransferase from its apoenzyme. 19P Severin E S ES Dixon H B HB eng Journal Article England Biochem J 2984726R 0264-6021 0 Coenzymes 0 Phosphates EC 2.6.1.1 Aspartate Aminotransferases IM Animals Aspartate Aminotransferases Chemical Phenomena Chemistry Coenzymes Phosphates analysis Swine 1968 11 1 1968 11 1 0 1

1968 Biochemical Journal

129. The influence of chloride and other univalent inorganic anions on the visible-absorption spectrum of aspartate aminotransferase (Full text)

The influence of chloride and other univalent inorganic anions on the visible-absorption spectrum of aspartate aminotransferase 1. The influence of Cl(-), Br(-), NO(3) (-) and F(-) ions on the visible-absorption spectrum of deionized aspartate aminotransferase was investigated. 2. Except for F(-), these anions caused an increase of the extinction at 430mmu with a concomitant decrease of that at 362mmu. 3. The affinity constants for Cl(-) and NO(3) (-) ions were calculated by a procedure based

1968 Biochemical Journal

130. THE ULTRASTRUCTURAL LOCALIZATION OF THE ISOZYMES OF ASPARTATE AMINOTRANSFERASE IN MURINE TISSUES (Full text)

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

131. EFFECTS OF FIXATION AND SUBSTRATE PROTECTION ON THE ISOENZYMES OF ASPARTATE AMINOTRANSFERASE STUDIED IN A QUANTITATIVE CYTOCHEMICAL MODEL SYSTEM (Full text)

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

132. Nonidentity of the Aspartate and the Aromatic Aminotransferase Components of Transaminase A in Escherichia coli (Full text)

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

133. The interaction of aliphatic and aromatic dicarboxylic acids with aspartate aminotransferase. (Full text)

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

134. The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with pepsin and trypsin (Full text)

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

135. Interaction of aspartate aminotransferase with amino acids (Full text)

Interaction of aspartate aminotransferase with amino acids 1. The capacity of various amino acids to convert the pyridoxal form of aspartate aminotransferase into the pyridoxamine form has been investigated. 2. Glutamate has the highest converting capacity; aspartate, alpha-aminopimelate, alpha-aminoadipate and other amino acids follow. 3. The converting capacity of the various amino acids assayed is connected with their structural features. 4. A possible role of amino acids as secondary (...) substrates of aspartate aminotransferase is suggested.

1965 Biochemical Journal

136. The nature of the multiple forms of cytoplasmic aspartate aminotransferase from pig and sheep heart (Full text)

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

137. Effect of pH, ionic strength and univalent inorganic ions on the reconstitution of aspartate aminotransferase (Full text)

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

138. The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastase (Full text)

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

139. Purification and some properties of cytoplasmic aspartate aminotransferase from sheep liver (Full text)

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

140. Studies on the changes in protein fluorescence and enzymic activity of aspartate aminotransferase on binding of pyridoxal 5′-phosphate (Full text)

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

To help you find the content you need quickly, you can filter your results via the categories on the right-hand side >>>>