Rat liver glutamyl ribonucleic acid synthetase. I. Purification and evidence for separate enzymes for glutamic acid and glutamine.

نویسنده

  • M P Deutscher
چکیده

Glutamyl ribonucleic acid synthetase was purified approximately 150-fold from homogenates of rat liver to a specific activity of 60 mpmoles of glutamyl-RNA formed per min per mg of protein. The enzyme at this stage of purification was judged to be about 40% pure, but in a state of aggregation. Although the enzyme was quite stable to storage, it was very heat labile, and lost activity during its assay. The purified enzyme required Mg++, adenosine triphosphate, L-glutamate, and soluble RNA for activity. Evidence is presented for the existence of distinct enzymes for glutamyl-RNA and glutaminyl-RNA formation. A rapid method for obtaining pure soluble RNA from liver is also described.

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

Mutants of Escherichia coli K-12 with an altered glutamyl-transfer ribonucleic acid synthetase.

Three streptomycin-suppressible lethal mutants of Escherichia coli K-12 have been shown to possess structurally altered glutamyl-transfer ribonucleic acid (tRNA) synthetases. Each mutant synthetase displays a K(m) value for glutamate which is 10-fold higher than the parental value, and the mutations reside in two widely separate loci on the genetic map. Mixing of the mutant extracts in pairs ga...

متن کامل

Glutamine synthetase from rat liver. Purification, properties, and preparation of specific antisera.

As the initial aspect of investigations on the regulation of glutamine synthetase in rat hepatomas and in hepatoma cell culture systems, glutamine synthetase from rat liver was purified to apparent homogeneity. A single protein band is found in gels after electrophoresis in three separate systems, and a constant enzyme specific activity is found in fractions containing glutamine synthetase acti...

متن کامل

Purification and Substrate Specificity of Arginyl-ribonucleic Acid Synthetase from Rat Liver.

It is generally accepted that in the first phase of protein biosynthesis, amino acid-specific enzymes, the aminoacyl-ribonucleic acid synthetases, carry out the activation of the various amino acids, and that the exacting specificity of these enzymes extends to the transfer of the amino acid to a particular soluble ribonucleic acid. Several investigators (l-5) have achieved the purification of ...

متن کامل

Purification, characterization, and expression of multiple glutamine synthetases from Prevotella ruminicola 23.

The Prevotella ruminicola 23 genome encodes three different glutamine synthetase (GS) enzymes: glutamine synthetase I (GSI) (ORF02151), GSIII-1 (ORF01459), and GSIII-2 (ORF02034). GSI, GSIII-1, and GSIII-2 have each been heterologously expressed in and purified from Escherichia coli. The subunit molecular mass of GSI was 56 kDa, while GSIII-1 and GSIII-2 were both 83 kDa. Optimal conditions for...

متن کامل

Activity of Liver Glutamine Transaminase toward L-Y -Glutamyl Hydrazones of aXeto Acids*

Rat liver glutamine transaminase acts on y-glutamyl hydrazones of a-keto acids to yield the corresponding L-amino acids and 3-hydroxy-tetrahydro-6-pyridazinone-3-carboxyllc acid; the latter compound undergoes nonenzymatic dehydration in acid to yield 1,4,5,6-tetrahydro-6-pyridazinone -3carboxylic acid. L-Amino acid oxidase (snake venom) also catalyzes the formation of 3-hydroxy-tetrahydro-6-pyr...

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 242 6  شماره 

صفحات  -

تاریخ انتشار 1967