Secretion and contraluminal uptake of dicarboxylic acids in the proximal convolution of rat kidney

1984 ◽  
Vol 400 (3) ◽  
pp. 241-249 ◽  
Author(s):  
K. J. Ullrich ◽  
H. Fasold ◽  
G. Rumrich ◽  
S. Kl�ss
Keyword(s):  
Rat Kidney ◽  
Dicarboxylic Acids ◽  
Proximal Convolution

Reabsorption of dicarboxylic acids from the proximal convolution of rat kidney

1983 ◽  
Vol 399 (1) ◽  
pp. 18-28 ◽  
Author(s):  
Eamonn Sheridan ◽  
Gerhard Rumrich ◽  
Karl J. Ullrich
Keyword(s):  
Rat Kidney ◽  
Dicarboxylic Acids ◽  
Proximal Convolution

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.

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