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Aspartate Aminotransferase

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101. Performance of the aspartate aminotransferase-to-platelet ratio index for the staging of hepatitis C-related fibrosis: an updated meta-analysis. (Full text)

Performance of the aspartate aminotransferase-to-platelet ratio index for the staging of hepatitis C-related fibrosis: an updated meta-analysis. The aspartate aminotransferase-to-platelet ratio index (APRI), a tool with limited expense and widespread availability, is a promising noninvasive alternative to liver biopsy for detecting hepatic fibrosis. The objective of this study was to update the 2007 meta-analysis to systematically assess the accuracy of APRI in predicting significant fibrosis

2011 Hepatology

102. Genome-wide association study identifies genetic variants in GOT1 determining serum aspartate aminotransferase levels (Full text)

Genome-wide association study identifies genetic variants in GOT1 determining serum aspartate aminotransferase levels We carried out a genome-wide association study of serum aspartate aminotransferase (AST) activity in 866 Amish participants of the Heredity and Phenotype Intervention Heart Study and identified significant association of AST activity with a cluster of single nucleotide polymorphisms located on chromosome 10q24.1 (peak association was rs17109512; P=2.80E-14), in the vicinity

2011 Journal of Human Genetics

103. MOLECULAR MODELING AND FUNCTIONAL CONFIRMATION OF A PREDICTED FATTY ACID BINDING SITE OF MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE (Full text)

MOLECULAR MODELING AND FUNCTIONAL CONFIRMATION OF A PREDICTED FATTY ACID BINDING SITE OF MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE Molecular interactions are necessary for proteins to perform their functions. The identification of a putative plasma membrane fatty acid transporter as mitochondrial aspartate aminotransferase (mAsp-AT) indicated that the protein must have a fatty acid binding site. Molecular modeling suggests that such a site exists in the form of a 500-Å(3) hydrophobic cleft

2011 Journal of Molecular Biology

104. Isolated elevated aspartate aminotransferase: a surprising outcome for clinicians. (PubMed)

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

105. Correlations of Complete Blood Count with Alanine and Aspartate Transaminase in Chinese Subjects and Prediction Based on Back-Propagation Artificial Neural Network (BP-ANN) (Full text)

Correlations of Complete Blood Count with Alanine and Aspartate Transaminase in Chinese Subjects and Prediction Based on Back-Propagation Artificial Neural Network (BP-ANN) BACKGROUND The complete blood count (CBC) is the most common examination used to monitor overall health in clinical practice. Whether there is a relationship between CBC indexes and alanine transaminase (ALT) and aspartate aminotransferase (AST) has been unclear. MATERIAL AND METHODS In this study, 572 normal-weight and 346

2017 Medical science monitor : international medical journal of experimental and clinical research

106. Research Study Comparing a New Medicine "Fast-acting Insulin Aspart" to Another Already Available Medicine "NovoRapid"/"NovoLog" in People With Type 2 Diabetes

] Measured in appropriate SI unit Change from baseline in aspartate aminotransferase (AST) [ Time Frame: Week 0, week 16 ] Measured in appropriate SI unit Change from baseline in albumin [ Time Frame: Week 0, week 16 ] Measured in appropriate SI unit Change from baseline in alkaline phosphatase [ Time Frame: Week 0, week 16 ] Measured in appropriate SI unit Change from baseline in creatinine [ Time Frame: Week 0, week 16 ] Measured in appropriate SI unit Change from baseline in potassium [ Time Frame (...) Research Study Comparing a New Medicine "Fast-acting Insulin Aspart" to Another Already Available Medicine "NovoRapid"/"NovoLog" in People With Type 2 Diabetes Research Study Comparing a New Medicine "Fast-acting Insulin Aspart" to Another Already Available Medicine "NovoRapid"/"NovoLog" in People With Type 2 Diabetes - Full Text View - ClinicalTrials.gov Hide glossary Glossary Study record managers: refer to the if submitting registration or results information. Search for terms x × Study

2017 Clinical Trials

107. The Association between Fruit and Vegetable Intake and Liver Enzymes (Aspartate and Alanine Transaminases) in Tehran, Iran (Full text)

function enzymes.This cross-sectional study was conducted on 265 Tehrani healthy adults. Fruit and vegetable intake was assessed by a 147-items semi-quantitative food frequency questionnaire. Serum glucose, lipids, liver enzymes (alanine aminotransferase (ALT), aspartate aminotransferase (AST)), hs-Crp and body composition were measured in a fasting state.The mean age (± SD) of the participants was 35 ± 8.78. In the higher quartiles of vegetable intake, low-density lipoprotein (LDL) serum and total (...) The Association between Fruit and Vegetable Intake and Liver Enzymes (Aspartate and Alanine Transaminases) in Tehran, Iran Intake of fiber and antioxidants and following hypocaloric diets has beneficial effects on reduction of the liver enzymes. Fruits and vegetables are low in calorie and rich in fiber and antioxidants. There are few studies about special dietary effects on liver function. The aim of this study was to evaluate the association between fruit and vegetables intake and liver

2017 Ethiopian journal of health sciences

108. A 38 Week Trial Comparing Effect and Safety of Insulin Degludec/Insulin Aspart vs. Insulin Glargine Plus Insulin Aspart in Subjects With Type 2 Diabetes Treated With Basal Insulin With or Without Oral Antidiabetic Treatment in Need of Treatment Intensific

A 38 Week Trial Comparing Effect and Safety of Insulin Degludec/Insulin Aspart vs. Insulin Glargine Plus Insulin Aspart in Subjects With Type 2 Diabetes Treated With Basal Insulin With or Without Oral Antidiabetic Treatment in Need of Treatment Intensific A 38 Week Trial Comparing Effect and Safety of Insulin Degludec/Insulin Aspart vs. Insulin Glargine Plus Insulin Aspart in Subjects With Type 2 Diabetes Treated With Basal Insulin With or Without Oral Antidiabetic Treatment in Need (...) of Treatment Intensification - Full Text View - ClinicalTrials.gov Hide glossary Glossary Study record managers: refer to the if submitting registration or results information. Search for terms x × Study Record Detail Saved Studies Save this study Warning You have reached the maximum number of saved studies (100). Please remove one or more studies before adding more. A 38 Week Trial Comparing Effect and Safety of Insulin Degludec/Insulin Aspart vs. Insulin Glargine Plus Insulin Aspart in Subjects With Type

2016 Clinical Trials

109. The sequences of the coenzyme-binding peptide in the cytoplasmic and the mitochondrial aspartate aminotransferases from sheep liver. (Full text)

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

110. The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues. (Full text)

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

111. The anomalous kinetics of coupled aspartate aminotransferase and malate dehydrogenase. Evidence for compartmentation of oxaloacetate. (Full text)

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

112. Purification and general properties of aspartate aminotransferase of ox heart (Full text)

Purification and general properties of aspartate aminotransferase of ox heart 1. A five-step procedure for preparing highly purified aspartate aminotransferase from ox heart is described. 2. The homogeneity of the pure enzyme was established by criteria such as ultracentrifugation and electrophoresis in starch gel and in polyacrylamide gel. 3. The pure enzyme has an isoelectric point of about pH5, and E(1%) (1cm.) 14.40 at 278mmu. 4. The molecular weight of the pure enzyme was determined

1966 Biochemical Journal

113. Amino acid composition and terminal residues of aspartate aminotransferase from ox heart (Full text)

Amino acid composition and terminal residues of aspartate aminotransferase from ox heart 1. The amino acid composition of highly purified aspartate aminotransferase from ox heart was determined. 2. Alanine is the only N-terminal residue. 3. Leucine was identified as the only C-terminal residue. 4. No disulphide bridges are present in the enzyme molecule. 5. The thiol groups are not equally accessible, the accessibility being comparatively easier in the apoenzyme molecule.

1966 Biochemical Journal

114. Acylation of aspartate aminotransferase (Full text)

Acylation of aspartate aminotransferase 1. Acetylation of aspartate aminotransferase from pig heart inhibits completely the enzymic activity when the coenzyme is in the amino form (pyridoxamine phosphate) or when the coenzyme has been removed, but not when the coenzyme is in the aldehyde form (pyridoxal phosphate). 2. The group the acylation of which is responsible for the inhibition has been identified with the in-amino group of a lysine residue at the coenzyme-binding site. Moreover

1967 Biochemical Journal

115. Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. (Full text)

Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. Two new mutations are described which, together, eliminate essentially all the aminotransferase activity required for de novo biosynthesis of tyrosine, phenylalanine, and aspartic acid in a K-12 strain of Escherichia coli. One mutation, designated tyrB, lies at about 80 min on the E. coli map and inactivates the "tyrosine-repressible" tyrosine/phenylalanine aminotransferase. The second mutation, aspC (...) , maps at about 20 min and inactivates a nonrespressible aspartate aminotransferase that also has activity on the aromatic amino acids. In ilvE- strains, which lack the branched-chain amino acid aminotransferase, the presence of either the tyrosine-repressible aminotransferase or the aspartate aminotransferase is sufficient for growth in the absence of exogenous tyrosine, phenylalanine, or aspartate; the tyrosine-repressible enzyme is also active in leucine biosynthesis. The ilvE gene product alone

1977 Journal of bacteriology

116. Mapping of the aspartate and aromatic amino acid aminotransferase genes tyrB and aspC. (Full text)

Mapping of the aspartate and aromatic amino acid aminotransferase genes tyrB and aspC. Co-transduction experiments using P1-mediated reciprocal and three-factor crosses have been used to map two mutations affecting the aspartate and aromatic amino acid aminotransferases of Escherichia coli. tyrB-, which inactivates the tyrosine-repressible component of these activities is co-transducible with metA and malB; the gene order is metA-malB-tyrB. aspC-, which inactivates the nonrepressible (...) aminotransferase with high activity for aspartate, maps between and is co-transducible with serC and pyrD.

1977 Journal of bacteriology

117. Selective permeability of rat liver mitochondria to purified aspartate aminotransferases in vitro. (Full text)

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

118. Interaction of aspartate aminotransferase with mercurochrome. Relationship of an exposed thiol group of the enzyme to the active centre. (Full text)

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

119. Genetic Analysis of Aspartate Aminotransferase Isozymes from Hybrids between DROSOPHILA MELANOGASTER and DROSOPHILA SIMULANS and Mutagen-Induced Isozyme Variants (Full text)

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

120. Syncatalytic conformational changes in aspartate aminotransferase determined by hydrogen-deuterium exchange. (Full text)

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

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