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|Title:||Microheterogeneity of molecular forms of arginase in mammalian tissues|
Reddy, S R R
kinetic and physical properties
activation by antibodies
|Abstract:||Two isoforms of arginase, A<sub>1</sub> and A<sub>2</sub>, were found in rat liver, submaxillary gland and kidney as well as beef kidney. In beef liver, however, A<sub>2 </sub> was the only detectable form. Two additional forms, A<sub>3 </sub> and A<sub>4 </sub>, found only in rat kidney were probably artifactitious. A<sub>1</sub> and A<sub>2</sub> exhibited chromatographic and immunological microheterogeneity. While A<sub>1</sub> in rat liver and submaxillary gland was excluded by DEAE-cellulose (pH 8.3) and retained on CM-cellulose (pH 7.5), that (A’<sub>1</sub>) in beef and rat kidneys was excluded by both ion-exchangers. A<sub>2</sub>in all tissues was retained on DEAE-cellulose, but not on CM-cellulose. Both A<sub> 1</sub>and A<sub>2 </sub> in rat liver and beef kidney, A<sub>1</sub> from rat submaxillary gland and A<sub>2 </sub> from beef liver were precipitated by antibodies to rat and beef liver arginases. None of the forms in rat kidney (A<sub>1</sub>, A<sub>2 </sub>, A<sub>3 </sub> and A<sub>4 </sub>) showed any cross-reactivity to either antibody. Rat submaxillary gland A<sub>2 </sub> was precipitated by anti-rat liver arginase, but activated by anti-beef liver arginase. While the major molecular forms were A<sub>1 </sub> in rat liver and submaxillary gland and A<sub>2 </sub> in beef liver and rat kidney, the two forms occurred in equal proportions in beef kidney. It appears that different isoforms might function as components of the urea cycle in the liver of different mammals and of the arginine catabolic pathway in different extrahepatic tissues.|
|Appears in Collections:||IJBB Vol.40(6) [December 2003]|
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