A heritable variant of mouse liver ornithine aminotransferase (EC 2.6.1.13) induced by ethylnitrosourea.

نویسندگان

  • C S Giometti
  • S L Tollaksen
  • M A Gemmell
  • J Burcham
  • C Peraino
چکیده

A variant of ornithine aminotransferase (OAT, EC 2.6.1.13) has been detected in an offspring of a male mouse treated with ethylnitrosourea. The evidence presented to support the identification of the protein variant (ENU 2) as altered OAT includes (a) a corresponding 50% decrease in the abundance of a protein, located one charge unit basic to the variant, which comigrates on two-dimensional gel patterns with purified mouse liver OAT; (b) the binding of anti-rat-OAT antibody to the variant; (c) the increased abundance of the variant protein in the livers of mice fed a high protein diet (85% casein); and (d) purification of the variant through an OAT purification protocol.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Alterations in enzymes of amino acid catabolism in livers of rats bearing the Morris 7800 hepatoma.

The activities of the amino acid-catabolizing enzymes, serine dehydratase (EC 4.2.1.16), ornithine aminotransferase (EC 2.6.1.13), tyrosine aminotransferase (EC 2.6.1.5), and alanine aminotransferase (EC 2.6.1.12), were measured in the livers of rats bearing the Morris 7800 hepatoma for varying periods. A relatively rapid decrease in the activities of hepatic serine dehydratase and orni thine a...

متن کامل

In vitro synthesis and processing of a precursor to ornithine aminotransferase.

Poly(A)+ RNA was isolated from liver-free polysomes of rats maintained on a 60% casein diet by sodium dodecyl sulfate-phenol-chloroform extraction and oligo(dT)-cellulose chromatography. Poly(A)+ RNA translated in a rabbit reticulocyte lysate system produced a polypeptide of 49,000 daltons that was immunoprecipitated by monospecific, affinity-purified IgG antibodies to ornithine aminotransferas...

متن کامل

Interactions of diet and cortisone in the regulation of adaptive enzymes in rat liver.

The responses of the adaptive enzymes, serine dehydrase (L-serine hydro-lyase (deaminating), EC 4.2.1.13), ornithine transaminase (L-ornithine:2-oxoacid aminotransferase, EC 2.6.1.13), glucose 6-phosphate dehydrogenase (D-ghCOSe 6-phosphate:NADP oxidoreductase, EC 1.1.1.49), and glucokinase (ATP:o-glucose 6-phosphotransferase, EC 2.7.1.2), in rat liver were studied in relation to changes in the...

متن کامل

Regulation of ornithine aminotransferase in rat kidney by estradiol and pyridoxine.

Increased synthesis of ornithine aminotransferase [EC 2.6.1.13] (OAT) in the kidney of pyridoxine-deficient rats has been reported previously (Ikeda, M. and Okada, M. (1985): J. Nutr. Sci. Vitaminol., 31, 553-561). In this report the effects of 3,3',5'-triiodothyronine (T3) and estradiol on OAT activity in the kidney of rats given pyridoxine-deficient and control diets were studied. T3 induced ...

متن کامل

Immunochemical studies of serine dehydratase and ornithine aminotransferase regulation in rat liver in vivo.

Previous studies of serine dehydratase (EC 4.2.1.13) and ornithine aminotransferase (EC 2.6.1.13) adaptation in rat liver showed that in rats on a high protein diet, glucocorticoid administration increased serine dehydratase activity while simultaneously reducing the activity of ornithine aminotransferase. The present study examines the role of enzyme synthesis in the expression of these and ot...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 263 30  شماره 

صفحات  -

تاریخ انتشار 1988