Efficient in vitro expression of interferon α analogs using SP6 polymerase and rabbit reticulocyte lysate

1988 ◽  
Vol 5 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Martin J. Tymms ◽  
Beth McInnes
Keyword(s):  
Rabbit Reticulocyte Lysate ◽  
Interferon Α ◽  
In Vitro Expression ◽  
Reticulocyte Lysate

Cloning, in vitro expression and bioactivity of goose interferon-α

Cytokine ◽  
2006 ◽  
Vol 34 (3-4) ◽  
pp. 177-183 ◽  
Author(s):  
Hong-Tao Li ◽  
Bo Ma ◽  
Jing-Wei Mi ◽  
Hong-Yan Jin ◽  
Li-Na Xu ◽  
...  
Keyword(s):  
Interferon Α ◽  
In Vitro Expression

scholarly journals Seed extracts inhibiting protein synthesis in vitro

1980 ◽  
Vol 186 (2) ◽  
pp. 439-441 ◽  
Author(s):  
A Gasperi-Campani ◽  
L Barbieri ◽  
P Morelli ◽  
F Stirpe
Keyword(s):  
Protein Synthesis ◽  
Rabbit Reticulocyte Lysate ◽  
Intact Cells ◽  
Euonymus Europaeus ◽  
Lower Extent ◽  
Reticulocyte Lysate ◽  
Dialysis Membranes ◽  
Inhibiting Protein ◽  
Seed Extracts

Of 33 seed extracts examined, 12 inhibited protein synthesis in a rabbit reticulocyte lysate. This activity seems to be due to a protein, since (i) it was recovered with the (NH4)2SO4 precipitate, (ii) it was retained by dialysis membranes, and (iii) in all cases but one was destroyed by boiling. Only the extracts from the seeds of Adenia digitata and, to a lower extent, of Euonymus europaeus inhibited protein synthesis in intact cells.

scholarly journals Unusual ciliate-specific codons in Tetrahymena mRNAs are translated correctly in a rabbit reticulocyte lysate supplemented with a subcellular fraction from Tetrahymena

1987 ◽  
Vol 244 (2) ◽  
pp. 331-335 ◽  
Author(s):  
P H Andreasen ◽  
H Dreisig ◽  
K Kristiansen
Keyword(s):  
Codon Usage ◽  
Genetic Code ◽  
Subcellular Fraction ◽  
Tetrahymena Thermophila ◽  
Rabbit Reticulocyte Lysate ◽  
Reading Frame ◽  
Universal Genetic Code ◽  
Reticulocyte Lysate ◽  
Translational Termination

The codon usage of Tetrahymena thermophila and other ciliates deviates from the ‘universal genetic code’ in that UAA and probably UAG are not translational termination signals but code for glutamine. Therefore, translation in vitro of mRNA from Tetrahymena in a reticulocyte lysate is prematurely terminated if a UAA or UAG triplet is present in the reading frame of the mRNA. We show that the addition of a subcellular fraction from Tetrahymena thermophila enables a rabbit reticulocyte lysate to translate Tetrahymena mRNAs into full-sized proteins. The activity of the subcellular fraction is shown to depend on the combined function of a protein component(s) and a tRNA(s). The subcellular fraction is easily prepared and its usefulness for the identification of isolated mRNAs from Tetrahymena by their translation products in vitro is demonstrated.

In Vitro Cleavage of eIF4GI but not eIF4GII by HIV-1 Protease and its Effects on Translation in the Rabbit Reticulocyte Lysate System

2002 ◽  
Vol 318 (1) ◽  
pp. 9-20 ◽  
Author(s):  
Théophile Ohlmann ◽  
Déborah Prévôt ◽  
Didier Décimo ◽  
Florence Roux ◽  
Jérôme Garin ◽  
...  
Keyword(s):  
Rabbit Reticulocyte Lysate ◽  
Rabbit Reticulocyte Lysate System ◽  
Reticulocyte Lysate ◽  
Hiv 1

scholarly journals Characterization of single-chain antibody (sFv)-toxin fusion proteins produced in vitro in rabbit reticulocyte lysate.

1993 ◽  
Vol 268 (7) ◽  
pp. 5302-5308
Author(s):  
P.J. Nicholls ◽  
V.G. Johnson ◽  
S.M. Andrew ◽  
H.R. Hoogenboom ◽  
J.C. Raus ◽  
...  
Keyword(s):  
Fusion Proteins ◽  
Rabbit Reticulocyte Lysate ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Reticulocyte Lysate

INDUCTION OF SPECIFIC TRANSLATABLE MESSENGER RNA'S BY OESTROGEN AND PROGESTERONE

1972 ◽  
Vol 71 (2_Suppla) ◽  
pp. S381-S395 ◽  
Author(s):  
Bert W. O'Malley ◽  
Gary C. Rosenfeld ◽  
John P. Comstock ◽  
Anthony R. Means
Keyword(s):  
De Novo ◽  
Rabbit Reticulocyte Lysate ◽  
System Synthesis ◽  
Reticulocyte Lysate

ABSTRACT In this manuscript, we report the de novo synthesis of two specific chick proteins, ovalbumin and avidin, in a heterologous rabbit reticulocyte lysate in vitro system. Synthesis of these proteins is absolutely dependent on RNA extracted from oviduct and not RNA extracted from non-target tissues. Furthermore, we have demonstrated that the intracellular accumulations of ovalbumin mRNA and avidin mRNA are directly dependent upon prior stimulation by oestrogen and progesterone, respectively.

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