닭 간에서 ornitine aminotransferase는 주로 mitochondrial fraction에 존재하였다. 이 효소를 열처리, ammonium sulfate fractionation, DEAE-cellulose ion exchange chromatography, Sephadex G-200 filtration, CM-Sephadex column chromatography를 이용하여 정제해서 disc polyacrylamide gel electrophoresis를 하였더니 하나의 단백질 띠가 얻어졌다. 이 정제된 효소를 이용해서 몇가지 성질을 조사해본 결과는 다음과 갈다. SDS-polyacrylamide gel electrophoresis에 의해 측정된 분자량은 62,000이었고 gel filtration에 의한 값은 63,000이었으므로 이 효소는 monomer로 존재한다고 생각되었다. L-ornithine과 $alpha$-ketoglutarate에 대한 $K_m$ 값은 각각 6.31 mM, 1, 03 mM 이였으며, 이 효소는 기질의 농도가 높을 때 저해되었고 또한 3 mM p-chloromercuriphenylsulfonic acid를 가해주면 80% 저해되었다. glyoxylate, oxaloacetate, pyruvate도 L-ornithine보다는 못하지만 amino group acceptor로서 작용하였으며, 효소활성에 대한 최적 pH는 7.3으로 측정되었다.
Ornithine aminotransferase was purified from chicken liver and several properties of the enzyme were studied. The purified enzyme appeared to be homogeneous on polyacrylamide gel electrophoresis with and without SDS. The molecular weight of the enzyme was estimated as 62,000 by SDS-polyacrylamide gel electrophoresis, and as 63,000 by gel filtration. The $K_m$ values for ornithine and $alpha$-ketoglutarate were found to be 6.31 mM and 1.03 mM, respectively. The enzyme was inhibited either by high substrate concentrations or by p-chloromercuriphenylsulfonic acid. Glyoxylate, oxaloacetate and pyruvate could act as amino group acceptors, but they were much less effective than $alpha$-ketoglutarate. Optimum pH of this enzyme was found to be 7.3.
