A variant of ornithine aminotransferase from mouse small intestine.
- Author:
Seong Nam LIM
1
;
Hye Won RHO
;
Jin Woo PARK
;
Eun Chung JHEE
;
Jong Suk KIM
;
Hyung Rho KIM
Author Information
1. Dental School, Chonbuk National University, Chonju, Korea.
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
ornithine aminotransferase;
mouse;
small intestine
- MeSH:
Amino Acid Sequence;
Animal;
Intestine, Small/enzymology*;
Liver/enzymology;
Male;
Mice;
Mice, Inbred ICR;
Molecular Sequence Data;
Molecular Weight;
Ornithine-Oxo-Acid Transaminase/metabolism*;
Ornithine-Oxo-Acid Transaminase/isolation & purification;
Ornithine-Oxo-Acid Transaminase/genetics*;
Tissue Distribution;
Trypsi
- From:Experimental & Molecular Medicine
1998;30(3):131-135
- CountryRepublic of Korea
- Language:English
-
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 alpha-ketoglutarate, were similar to those of hepatic OAT. However, intestinal OAT was more labile than hepatic OAT to tryptic digestion.
