Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.6.1.1 (aspartate aminotransferase)
 21,665 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In seven patients with implanted intermedics NOVA MR pacemakers, we examined the cardiopulmonary effects of maximum bicycle ergometer exercise for three types of pacing in a randomized sequence: VVI or AAI at 70/min (SSI 70), rate adaptive temperature controlled with the implanted NOVA MR, and rate adaptive activity controlled by means of a Medtronic Activitrax pacemaker taped to the chest wall, which triggered the implanted Nova MR in the VVT or AAT mode via skin electrodes. The maximum exercise tolerance was 67 W with SSI 70, 71 W with Activitrax and 91 W with Nova MR. The maximum oxygen uptake was accordingly 17.6 ml/min/kg with SSI 70, 19.5 ml/min/kg with Activitrax, and 21.5 ml/min/kg with Nova MR. The highest heart rate reached was 81 beats/min with SSI 70,98 beats/min with Activitrax and 118 beats/min with Nova MR. The rate increase from rest to maximum exercise was 11 beats/min with SSI 70,29 beats/min with Activitrax and 47 beats/min with Nova MR. An increase in exercise tolerance and maximum heart rate could be achieved with both rate adaptive types of pacing, but significantly more clearly with the temperature controlled Nova MR than with the activity controlled Activitrax. However, using a different form of exercise, e.g. treadmill ergometry, the rate response of the Activitrax would presumably have been somewhat clearer.
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PMID:[Cardiopulmonary stress test in variable frequency stimulation: a comparison of Activitrax and Nova-MR pacemakers in VVI/AAI stimulation]. 306 57

We examined the cardiopulmonary effects of maximum bicycle ergometer exercise in seven patients with implanted Intermedics Nova MR pacemakers for three types of pacing in a randomized sequence: VVI or AAI at 70 beats/min (SSI 70), rate-adaptive temperature-controlled pacing with the implanted Nova MR, and rate-adaptive activity-controlled pacing with a Medtronic Activitrax pacemaker taped to the chest wall, which triggered the implanted Nova MR in the VVT or AAT mode by skin electrodes. The maximum exercise tolerance was 67 W with SSI 70, 71 W with Activitrax pacing, and 91 W with Nova MR pacing; the maximum oxygen uptake as 17.6, 19.5, and 21.5 ml/min/kg, respectively. The highest heart rate achieved was 81 beats/min with SSI 70, 98 beats/min with the Activitrax, and 118 beats/min with the Nova MR on average; the mean rate increase from rest to maximum exercise was 11, 29, and 47 beats/min, respectively. With both rate-adaptive types of pacing (Nova MR and Activitrax), an increase in exercise tolerance and maximum heart rate could be achieved, but this increase was significantly more obvious with the temperature-controlled Nova MR than with the activity-controlled Activitrax. However, with a different form of exercise, for example, treadmill ergometry, the rate response of the Activitrax would presumably have been somewhat clearer.
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PMID:First clinical results with a new temperature-controlled rate-responsive pacemaker. Comparison of Activitrax and Nova MR pacemakers with VVI/AAI pacing. 318 Mar 90

Cytosolic and mitochondrial isoenzymes of aspartate aminotransferase (EC 2.6.1.1) were purified to homogeneity from chicken liver, without previous fractionation of the subcellular components. The procedure includes initial heat treatment and ammonium sulfate fractionation. The two isoenzymes can then be separated by a DEAE-Sepharose chromatography using a linear gradient of L-aspartate (reaction substrate). The separated fractions can be further purified by a parallel step with HA-Ultrogel prior to octyl-Sepharose (c-AAT) and CM-Sepharose (m-AAT) chromatographies. Michaelis constants, pI values, inhibition by adipate and subforms generation with time were studied for both isoenzymes.
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PMID:Simultaneous purification and characterization of aspartate aminotransferase isoenzymes from chicken liver. 323 18

We have previously identified a unique site, pac, from which packaging of precursor concatameric viral DNA into proheads starts during the maturation process of bacteriophage CP-T1. The direction of this packaging was determined from restriction enzyme cleavage patterns of CP-T1 DNA. A restriction enzyme generated fragment containing pac was cloned and the surrounding DNA region sequenced. Analysis of the nucleotide sequence revealed numerous repeat regions related to the consensus sequence PuagttGAT.AAT.aa.t. Within the sequenced region an open reading frame encoding a 12260 Mr protein was also identified. This protein appears to share homology with the binding domains of known DNA binding proteins and may represent a putative Pac terminase possessing the specific endonuclease activity required for cleavage at the pac site. Minicell analysis of deletion derivatives of the pac-containing clone revealed a protein of approximately 12,900 Mr encoded within this same region, confirming that this Pac protein is phage encoded.
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PMID:Molecular analysis of the packaging signal in bacteriophage CP-T1 of Vibrio cholerae. 341 20

A new purification method has been developed which only exploits the chromatographic behaviour of avian liver mitochondrial aspartate aminotransferase enzymes (m-AAT), and permits a rapid isolation of the protein (4 days) in large quantities with high yield and low cost. m-AAT from turkey, chicken and quail livers have been isolated by chromatography on CM-Sepharose, Sephadex G-100 and 5' AMP-Sepharose using TEA-acetate buffer (pH 7.4), and specific activities (A.E.) of 311.6, 318.9, 320.1 I.U./mg respectively were obtained. Preparations were homogeneous as judged by various electrophoretic techniques and by size exclusion HPLC. The amino acid composition, Stokes Radius, subunit molecular weight and pI values have been determined and compared, finding no appreciable differences among them. In contrast, the absorption spectrum of the turkey enzyme differed from those of chicken and quail at both pH 7.4 and pH 5.0.
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PMID:Purification and comparative studies of several mitochondrial aspartate aminotransferases from avian liver. 343 3

To evaluate the frequency of false positive globular inclusions, 89 autopsy cases with various malignancies and liver metastases have been examined by immunoperoxidase staining of liver sections and isoelectric focusing of sera. Four subjects with AAT globules in their hepatocytes were found, all of whom had the Pi Z phenotype. Globular inclusions were not found in any subject lacking the Pi Z allele on isoelectric focusing, but in 3 subjects with the Pi Z phenotype no hepatocytic globules were found.
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PMID:The Pi Z allele and hepatic alpha 1-antitrypsin globules in patients with secondary liver cancer. 348 14

Distributions of activity of the cytosolic (cAAT) and mitochondrial (mAAT) isoenzymes of aspartate aminotransferase and of malate dehydrogenase (MDH) were determined in guinea pig retinal layers. The distribution of total AAT activity (tAAT = cAAT + mAAT) and of mAAT activity correlated well (r = 0.88-0.91) with the distribution of MDH activity. mAAT activity was highest in the inner segments of the photoreceptors; there was a greater than twelve-fold difference between activity in that layer and in the inner retinal layers. cAAT activity was also highest in the inner segments, but the difference between the activity in the inner segments and the other layers was not nearly as great as with mAAT. cAAT activity was also relatively high in the outer nuclear layer, outer plexiform layer, and part of the inner plexiform layer. The high activity of cAAT, mAAT, and MDH in the inner segments indicates that all of these enzymes are involved in metabolic reactions related to energy production and/or to photoreceptive processes in the outer segments and, therefore, that the enzymes are probably involved in energy-related metabolism at synapses. However, other functions, including those related to neurotransmission, are not excluded.
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PMID:Distribution of activities of aspartate aminotransferase isoenzymes and malate dehydrogenase in guinea pig retinal layers. 357 59

The ontogenetic trends in the expression of 25 isozymes in liver, gizzard, heart, and pectoralis muscle of White Leghorn chickens were examined using starch gel electrophoresis. Little change in expression during development was evident in liver S-AAT-A, GPI-A, S-ICDH-A, S-MDH-A and M-MDH-A, in gizzard S-ACON-A, ADH-A, GPI-A, HK-1, HK-3, ME-A PEP-1, and PGM-A, in heart ADH-A, HK-1, HK-3, ME-A, PEP-2, PGM-A, and LDH-A, in pectoralis M-ACON-A, S-ACON-A, ADH-A, HK-1, HK-3, ME-A, PEP-2, and PGM-A, and in liver, gizzard, and heart M-ACON-A, ALD-A, CK-A, G3PDH-A, HK-1, and PGDH-A. Increasing levels of activity were demonstrated in liver ADH-A, ME-A, and PEP-2, in heart M-MDH-A, S-ICDH-A, M-ICDH, and M-AAT-A, and in pectoralis LDH-A, LDH-B, G3PDH-3, ALD-A, CK-A, HK-2, and PGM-B. There was a decrease in the activity of HK-1 in liver and in PEP-1 and PGDH-A in pectoralis muscle throughout development. While CK-C is active in the embryonic pectoralis, CK-A is restricted to later developmental stages. Isozyme expressions in regions of the pectoralis containing fast and slow muscle fibers in 7-month-posthatch individuals were noted and found to be identical. The results underscore the need to use similar developmental stages and tissue samples in comparative electrophoretic studies of birds.
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PMID:A survey of tissue-specific isozyme expressions during chicken ontogeny. 360 63

The effects of testosterone on mitochondrial aspartate aminotransferase (mAAT) synthesis in rat ventral prostate was investigated. Procedures for the isolation, purification and characterization of AAT isozymes were developed and described. Purified mAAT preparations contained no demonstrable contaminating proteins. Prostatic mAAT was characterized as a cationic protein with an estimated mol. wt of 120,000. Cytoplasmic AAT (cAAT) isozyme was identified as an anionic protein with an estimated mol. wt of 132,000. A cytosolic cationic isozyme, similar to mAAT, was also identified as pre-mAAT. Testosterone administration to castrated rats resulted in significant increases in leucine incorporation into mAAT, in the level of mAAT, and in mAAT activity. These effects of testosterone were observed within 2 h of administration. Conversely, testosterone administration had none of these effects on cAAT or on non-AAT protein pool. Testosterone treatment did appear to increase leucine incorporation into pre-mAAT. Testosterone treatment in organ cultures and in prostate epithelial cell cultures resulted in the same stimulatory effects on mAAT as observed in the in vivo studies. The hormone was effective at the physiological concentration of 2 X 10(-9) M. These results indicated that testosterone has a rapid and specific effect on the biosynthesis of mAAT. This continues to support our proposal that testosterone regulates prostate citrate production via a stimulatory effect on mAAT which results in increased mitochondrial synthesis of citrate from aspartate.
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PMID:Testosterone stimulation of mitochondrial aspartate aminotransferase levels and biosynthesis in rat ventral prostate. 365 47

The basic components of a data- and methodbase system useful for both individual diagnosis and (group-study) research in neuropsychology are described. Such a system enables one to organize, access and evaluate large data-sets of behavioural, neuroradiological and neurological information. The most important component of the system, the data- and methodbase management system, is described in some detail. It operates on databases comprised of Aachen Aphasia Test examinations and standardized CT evaluations as well as on methodbases containing various sets of analysis routines for the psychometric evaluation of (individual) aphasia test results and the evaluation and (graphical) presentation of standardized (individual) CT lesions. Although exemplified for AAT scores the techniques and principles employed are applicable to data- and methodbase systems in general.
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PMID:The design and application of a data- and methodbase system for the Aachen Aphasia Test. 365 58


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