Rabbit liver 3-hydroxyhexobarbital dehydrogenase. Purification and properties.

نویسندگان

  • R Takenoshita
  • S Toki
چکیده

3-Hydroxyhexobarbital dehydrogenase has been purified from the soluble fraction of rabbit liver. The enzyme gives the molecular weight of 42,000 by the method of sodium dodecyl sulfate-polyacrylamide gel disc electrophoresis and 33,000 by the Sephadex G-100 gel filtration method. Styrylmethylcarbinol, P-ionol, 1-indanol and I-tetralol are ako metabolized by the enzyme. Michaelis constants for 3-hydroxyhexobarbital are 5.3 X 10m4 M (with NAD+) and 4.0 X 10e4 M (with NADP+).

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

Guinea Pig Liver 3-Hydroxyhexobarbital Dehydrogenase*

3-Hydroxyhexobarbital dehydrogenase, which catalyzes the reversible oxidation of 3-hydroxyhexobarbital to d-oxohexobarbital, has been purified 47%fold from the soluble fraction of guinea pig liver with a yield of 47%. The specific activity of the purified enzyme is 9.4 units/mg of protein. Results of polyacrylamide gel disc electrophoresis and isoelectric focusing indicated that the purified en...

متن کامل

Purification and properties of rabbit muscle L-glycerol 3-phosphate dehydrogenase.

A modified procedure has been developed for the purification of rabbit muscle l-glycerol 3-phosphate dehydrogenase. The product of the preparation satisfies all criteria of homogeneity. Some physical properties of the enzyme have been re-investigated. The results suggest that previous preparations may have been contaminated with significant amounts of heavy-molecular-weight protein.

متن کامل

Purification and characterization of a protein inhibitor from rat

A protein inhibitor of HMG-CoA reductase phosphatase activity from rat liver was purified to homogeneity. The protein was purified 4,000-fold with an overall yield of 4%. The purified protein had a molecular mass of 31 kDa. This spontaneously active protein is thermostable and acid-resistant. The protein inhibitor is phosphorylated by glycogen synthase kinase-3 and CAMP-dependent protein kinase...

متن کامل

"Affinity" chromatography of steroid-transforming enzymes with a non-steroidal ligand.

The chromatographic behaviour of an avian oestradiol-17 beta dehydrogenase, the 3(17) beta-hydroxy steroid dehydrogenase from Pseudomonas testosteroni and cortisone reductase from Streptomyces dehydrogenans was studied on columns of p-(phenoxypropoxy)aniline attached to CNBr-activated Sepharose. The ligand was effective in adsorbing the oestradiol dehydrogenase from a partially purified extract...

متن کامل

Purification of nucleotide-requiring enzymes by immunoaffinity chromatography.

Monospecific (affinity-purified) anti-(yeast glucose-6-phosphate dehydrogenase) IgG inhibits three different NADPH-requiring enzymes, chicken liver dihydrofolate reductase, pigeon liver fatty acid synthetase and chicken liver malic enzyme. The inhibition of all three enzymes was approx. 50% in a 2h incubation with 100 micrograms of IgG. Similarly, with several different NADH-requiring enzymes, ...

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 249 17  شماره 

صفحات  -

تاریخ انتشار 1974