Labelling of Immunologically Specific Proteins by Ribonucleoprotein Particles From Rat-Liver and Chick-Liver Cell Sap

Deckena, Von Der

doi:10.1042/bj0880385

Cited by 17 publications

(2 citation statements)

References 31 publications

(19 reference statements)

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“…This is due to the presence in these tissues of a protein similar to albumin [6,7,9,10]. When applying appropriate purification procedures, Judah and Nicholls observed that liver slices continued to incorporate ['4C]leucine into albumin after incorporation into total protein had been interrupted by cycloheximide or excess unlabelled leucine [Ill.…”

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“…In contrast to the easy isolation from serum, rather extensive purification is required to obtain pure albumin from biological material involved in albumin synthesis, such as liver [l-41, hepatoma [2,3], hepatocyte suspensions [ 5 ] , and cell-free proteinsynthesizing systems from liver [6-81. This is due to the presence in these tissues of a protein similar to albumin [6,7,9,10]. When applying appropriate purification procedures, Judah and Nicholls observed that liver slices continued to incorporate ['4C]leucine into albumin after incorporation into total protein had been interrupted by cycloheximide or excess unlabelled leucine [Ill.…”

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The Kinetics in vivo of the Synthesis of Albumin‐Like Protein and Albumin in Rats

Urban

Chelladurai

Millership

et al. 1976

European Journal of Biochemistry

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The incorporation of radioactivity into total protein, albumin-like protein and albumin in liver, and into total protein and albumin in blood plasma, was studied for a time period of 2 h after intraportal injection of ~-[l-'~C]leucine.1. In the liver, radioactivity began to increase in albumin-like protein before 2.5 min and in albumin at about 10 min after injection. In the plasma, radioactive albumin appeared at about 15 min. No albumin-like protein could be detected in the plasma.2. Maximum radioactivity was reached first in albumin-like protein, then in hepatic albumin and finally in albumin in the blood-stream. The maximum specific radioactivity of albumin-like protein was 15 times higher than that of extravascular hepatic albumin which, in turn, was 6 times higher than that of plasma albumin.3. The increase of radioactivity in albumin in the blood corresponded almost quantitatively to the decrease of radioactivity in albumin-like protein.4. It is concluded that the albumin-like protein is the precursor of albumin in vivo. It is converted into albumin 5 -6 min before the appearance of newly synthesized albumin in the blood-stream.In contrast to the easy isolation from serum, rather extensive purification is required to obtain pure albumin from biological material involved in albumin synthesis, such as liver [l-41, hepatoma [2,3], hepatocyte suspensions [ 5 ] , and cell-free proteinsynthesizing systems from liver [6-81. This is due to the presence in these tissues of a protein similar to albumin [6,7,9,10]. When applying appropriate purification procedures, Judah and Nicholls observed that liver slices continued to incorporate ['4C]leucine into albumin after incorporation into total protein had been interrupted by cycloheximide or excess unlabelled leucine [Ill. This suggested that a precursor protein other than intrahepatic albumin is involved in the biosynthesis of serum albumin. Recently, a possible precursor protein, an albumin-like protein, was isolated from liver and characterised [12-141. It differed from albumin by a short peptide extension at the N-terminus. The earlier finding of identical Ntermini for albumin-like protein and albumin [15] can probably be explained by insufficient separation of the two proteins and difficulties in the determination of the N-terminal amino acid of the albumin-like protein.In this paper, we describe the kinetics in vivo of ['4C]leucine incorporation into total protein, albuminlike protein and albumin in the liver, and into total protein and albumin in the plasma. A quantitative analysis provides evidence that the albumin-like protein is a precursor in the synthesis of albumin in vivo. A preliminary report of this work appeared elsewhere P61. MATERIALS AND METHODS AnimalsInbred buffalo rats were kept at a room temperature of 23 "C and had free access to water and a diet containing about 20 % protein (Barastoc Mouse Breeder Ration, Barastoc Products, Melbourne, Australia). Only male rats were used. They were starved overnight and operated on between 9 a.m. and 2 p.m. ...

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The Kinetics in vivo of the Synthesis of Albumin‐Like Protein and Albumin in Rats

Urban

Chelladurai

Millership

et al. 1976

European Journal of Biochemistry

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Die Translation der genetischen Information am Ribosom

Schreiber

1971

Angewandte Chemie

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Die in der Basensequenz der Nucleinsäuren enthaltene Information für die Proteinstruktur wird am Ribosom in die Aminosäurensequenz der Proteine übersetzt. Diese Übersetzung, Translation genannt, läßt sich in den Kettenstart, die Kettenverlängerung und den Kettenabschluß gliedern. An jedem Abschnitt sind mehrere spezifische Proteinfaktoren und Nucleinsäuren beteiligt. – Beim Kettenstart werden aus der Startaminosäure‐tRNA, der mRNA mit dem Startsignal und der kleinen und großen Untereinheit eines Ribosoms Startkomplexe gebildet. Dabei wirken GTP und die Startfaktoren mit. – Bei der Kettenverlängerung wird in einem Reaktionszyklus jeweils eine Aminosäure aus der Bindung an die tRNA in eine Bindung in der Polypeptidkette überführt. Zunächst wird die zu inkorporierende Aminosäure als Aminoacyl‐tRNA an das Ribosom gebunden, wozu GTP und Proteinfaktoren erforderlich sind. Die anschließende Entstehung der Peptidbindung wird durch die Peptidyltransferase der großen Ribosomenuntereinheit katalysiert. Danach wird die nunmehr um eine Aminosäure verlängerte Peptidyl‐tRNA auf dem Ribosom von der Aminosäure‐Acceptorstelle A an die Peptidyl‐Donorstelle P verlagert. Hierzu sind ein weiterer Proteinfaktor und die Spaltung von GTP in GDP und Phosphat notwendig. – Der Kettenabschluß wird eingeleitet, sobald eines der drei Terminatortripletts UAA, UAG oder UGA auf der sich relativ zum Ribosom vom 5′‐ zum 3′‐Ende bewegenden mRNA das Ribosom erreicht. Die Ablösung der fertigen Polypeptidketten vom Ribosom hängt von den Ablösefaktoren ab. Vor dem Start einer neuen Polypeptidkette dissoziieren die Ribosomen in ihre Untereinheiten.

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Translation of Genetic Information on the Ribosome

Schreiber

1971

Angew. Chem. Int. Ed. Engl.

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Labelling of Immunologically Specific Proteins by Ribonucleoprotein Particles From Rat-Liver and Chick-Liver Cell Sap

Cited by 17 publications

References 31 publications

The Kinetics in vivo of the Synthesis of Albumin‐Like Protein and Albumin in Rats

The Kinetics in vivo of the Synthesis of Albumin‐Like Protein and Albumin in Rats

Die Translation der genetischen Information am Ribosom

Translation of Genetic Information on the Ribosome

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