|
KMID : 0620919980300030131
|
|
Experimental & Molecular Medicine
1998 Volume.30 No. 3 p.131 ~ p.135
|
|
|
A variant of ornithine aminotransferase from mouse small intestine
|
|
Hyung Rho Kim/Seong Nam Lim
Hye Won Rho/Jin Woo Park/Eun Chung Jhee/Jong Suk Kim/Hyung Rho Kim
|
|
|
Abstract
|
|
|
|
The ornithine aminotransferase (OAT) activity of mouse was found to be highest in the small intestine. The mitochondrial OAT from mouse small intestine was purified to homogeneity by the procedures including heart treatment, ammonium sulfate fractionation, octyl-Sepharose chromatography, and Sephadex G-150 gel filtration. Comparing to the amino acid sequence of mouse hepatic OAT, six N-terminal amino acid residues have been deleted in intestinal OAT. However, the subsequent sequence was identical with that of hepatic OAT. The molecular weights of both intestinal and hepatic OAT were estimated as 46 kDa by SDS-gel electrophoresis and as 92 kDa by gel filtration, indicating that both native OATs are dimeric. Biochemical properties of intestinal OAT, such as molecular weight, pH optimum and K(m) values for L-ornithine and α-ketoglutarate, were similar to those of hepatic OAT. However, intestinal OAT was more labile than hepatic OAT to tryptic digestion.
|
|
|
KEYWORD
|
|
|
ornithine aminotransferase, mouse, small intestine,
|
|
|
FullTexts / Linksout information
|
|
|
|
|
Listed journal information
|
|
    
|
|