scholarly journals Purification and properties of kynurenine aminotransferase from rat kidney

1991 ◽  
Vol 279 (2) ◽  
pp. 595-599 ◽  
Author(s):  
M R Mawal ◽  
A Mukhopadhyay ◽  
D R Deshmukh
Keyword(s):  
Rat Kidney ◽  
Dicarboxylic Acids ◽  
Supernatant Fraction ◽  
Subunit Structure ◽  
Mitochondrial Enzyme ◽  
Kynurenine Aminotransferase ◽  
Kidney Mitochondria ◽  
Purification And Properties ◽  
Single Protein ◽  
Degree Of Purification

Previous reports indicated that a single protein exhibits kynurenine aminotransferase (KAT) and alpha-aminoadipate aminotransferase (AadAT) activities. However, recently we discovered that KAT and AadAT activities are associated with two different proteins. KAT from rat kidney supernatant fraction was purified to electrophoretic homogeneity by (NH4)2SO4 fractionation, DEAE-Sephacel and hydroxyapatite chromatography. This procedure separated KAT from AadAT and improved the overall yield and the degree of purification over previously published methods. Some of the properties of purified KAT, such as Mr, subunit structure and the inhibition by dicarboxylic acids, were identical with those reported previously. However, the substrate specificity and pI of purified KAT were different from earlier reports. The same procedure can also be used to purify KAT from rat kidney mitochondria. These results support our earlier observation that KAT and AadAT activities are associated with two proteins and suggest that cytosolic KAT may be structurally similar to the mitochondrial enzyme.

scholarly journals Purification and properties of 2-aminoadipate: 2-oxoglutarate aminotransferase from bovine kidney

1989 ◽  
Vol 261 (3) ◽  
pp. 761-768 ◽  
Author(s):  
D R Deshmukh ◽  
S M Mungre
Keyword(s):  
Rat Kidney ◽  
Deae Cellulose ◽  
Dicarboxylic Acids ◽  
Structural Similarity ◽  
Appreciable Amount ◽  
Kinetic Properties ◽  
Bovine Kidney ◽  
Purification And Properties ◽  
Kidney Enzyme ◽  
Structural Differences

Previous studies with rat kidney preparations indicated that 2-aminoadipate aminotransferase (AadAT) and kynurenine aminotransferase (KAT) activities are properties of a single protein. We found that bovine kidney contains an appreciable amount of AadAT activity, but lacks KAT activity. AadAT from bovine and rat kidney extracts were purified to electrophoretic homogeneity. The purification procedure included fractionation with (NH1)2SO1, heat treatment, DEAE-cellulose chromatography and hydroxyapatite chromatography. Physical and kinetic properties, such as pH optima, Km for substrates, Mr, electrophoretic mobility and inhibition by dicarboxylic acids of bovine kidney AadAT, were similar to those of the rat kidney enzyme. However, bovine kidney AadAT differed from rat kidney AadAT in substrate specificity, amino acid composition and stability when stored. The titration curve of bovine kidney AadAT was also different from that of the rat kidney enzyme. The results suggest that bovine kidney AadAT may have some structural similarity to rat kidney AadAT and that the structural differences observed between the two enzymes may explain the absence of KAT activity in bovine kidney.

scholarly journals Two forms of aspartate aminotransferase in rat liver and kidney mitochondria

1968 ◽  
Vol 108 (4) ◽  
pp. 619-624 ◽  
Author(s):  
M. M. Bhargava ◽  
A. Sreenivasan
Keyword(s):  
Rat Liver ◽  
Aspartate Aminotransferase ◽  
High Speed ◽  
Rat Kidney ◽  
Liver Mitochondria ◽  
Supernatant Fraction ◽  
Rat Liver Mitochondria ◽  
Aminotransferase Activity ◽  
Kidney Mitochondria ◽  
Liver And Kidney

1. Butan-1-ol solubilizes that portion of rat liver mitochondrial aspartate aminotransferase (EC 2.6.1.1) that cannot be solubilized by ultrasonics and other treatments. 2. A difference in electrophoretic mobilities, chromatographic behaviour and solubility characteristics between the enzymes solubilized by ultrasonic treatment and by butan-1-ol was observed, suggesting the occurrence of two forms of this enzyme in rat liver mitochondria. 3. Half the aspartate aminotransferase activity of rat kidney homogenate was present in a high-speed supernatant fraction, the remainder being in the mitochondria. 4. A considerable increase in aspartate aminotransferase activity was observed when kidney mitochondrial suspensions were treated with ultrasonics or detergents. 5. All the activity after maximum activation was recoverable in the supernatant after centrifugation at 105000g for 1hr. 6. The electrophoretic mobility of the kidney mitochondrial enzyme was cathodic and that of the supernatant enzyme anodic. 7. Cortisone administration increased the activities of both mitochondrial and supernatant aspartate aminotransferases of liver, but only that of the supernatant enzyme of kidney.

scholarly journals Identification and purification of the reconstitutively active glutamine carrier from rat kidney mitochondria

1998 ◽  
Vol 333 (2) ◽  
pp. 285-290 ◽  
Author(s):  
Cesare INDIVERI ◽  
Giuseppe ABRUZZO ◽  
Italo STIPANI ◽  
Ferdinando PALMIERI
Keyword(s):  
Rat Kidney ◽  
Thiol Group ◽  
Protein Band ◽  
Carrier Protein ◽  
Transport Activity ◽  
Kidney Mitochondria ◽  
Carrier Mediated Transport ◽  
Sds Page ◽  
Single Protein ◽  
Mitochondrial Extract

The glutamine carrier from rat kidney mitochondria, solubilized in dodecyl octaoxyethylene ether (C12E8) and partly purified on hydroxyapatite, was identified and completely purified by Celite chromatography. On SDS/PAGE, the purified glutamine carrier consisted of a single protein band with an apparent molecular mass of 41.5 kDa. When reconstituted into liposomes, the glutamine carrier catalysed both the unidirectional flux of glutamine and the glutamine/glutamine countertransport, which were completely inhibitable by a mixture of pyridoxal 5´-phosphate and N-ethylmaleimide. The carrier protein was purified 474-fold with a recovery of 58% and a protein yield of 0.12% with respect to the mitochondrial extract. The glutamine carrier-mediated transport is quite specific for l-glutamine. l-Asparagine is the only other amino acid that is efficiently transported by the reconstituted carrier protein. d-Glutamine, l-glutamate and l-aspartate are very poor substrates. The transport activity was inhibited by several thiol-group and amino-group reagents.

scholarly journals Glutamate transprot in rat kidney mitochondria.

1983 ◽  
Vol 258 (3) ◽  
pp. 1735-1739
Author(s):  
A C Schoolwerth ◽  
K F LaNoue ◽  
W J Hoover
Keyword(s):  
Rat Kidney ◽  
Kidney Mitochondria

Carvedilol protects against cisplatin-induced oxidative stress, redox state unbalance and apoptosis in rat kidney mitochondria

2011 ◽  
Vol 189 (1-2) ◽  
pp. 45-51 ◽  
Author(s):  
M.A. Carvalho Rodrigues ◽  
J.L. Rodrigues ◽  
N.M. Martins ◽  
F. Barbosa ◽  
C. Curti ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Redox State ◽  
Rat Kidney ◽  
Kidney Mitochondria
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