A Simplified Procedure for Large Scale Preparation of Purified Animal DNA-Dependent RNA Polymerase

1973 ◽  
Vol 28 (9-10) ◽  
pp. 610-613 ◽  
Author(s):  
C. D. Schmincke ◽  
P. Hausen
Keyword(s):  
Rna Polymerase ◽  
High Purity ◽  
Gel Electrophoresis ◽  
Large Scale ◽  
Deae Cellulose ◽  
Large Scale Preparation ◽  
Calf Thymus ◽  
Low Salt ◽  
Scale Preparation ◽  
Simplified Procedure

Abstract A procedure is described for obtaining DNA-dependent RNA polymerase form B from calf thymus in high purity. The procedure includes homogenization in low salt, sedimentation of chromatin at 50 000 x g, adsorption to DEAE-cellulose in a batch procedure, DNA-agarose chromato­graphy, and chromatography on DEAE-Sephadex. Analyses of the preparation by band sedimentation and gel-electrophoresis indicate a high purity of the enzyme.

A RAPID METHOD FOR THE LARGE SCALE PREPARATION OF CALF THYMUS DEOXYRIBONUCLEATE

1958 ◽  
Vol 36 (1) ◽  
pp. 1115-1119
Author(s):  
R. O. Hurst
Keyword(s):  
Salt Solution ◽  
Large Scale ◽  
Potassium Thiocyanate ◽  
Aqueous Salt Solution ◽  
High Yield ◽  
Large Scale Preparation ◽  
Calf Thymus ◽  
Thymus Tissue ◽  
Scale Preparation ◽  
Concentrated Solution

Isolation of deoxyribonucleate from a concentrated solution of thymonucleoprotein has been achieved by disruption of the protein nucleate bond with potassium thiocyanate, adsorption of the protein on celite, and alcohol precipitation of the deoxyribonucleate from aqueous salt solution. Highly polymerized nucleate can be obtained readily from 1 lb of calf thymus tissue in high yield.

A RAPID METHOD FOR THE LARGE SCALE PREPARATION OF CALF THYMUS DEOXYRIBONUCLEATE

1958 ◽  
Vol 36 (11) ◽  
pp. 1115-1119 ◽  
Author(s):  
R. O. Hurst
Keyword(s):  
Salt Solution ◽  
Large Scale ◽  
Potassium Thiocyanate ◽  
Aqueous Salt Solution ◽  
High Yield ◽  
Large Scale Preparation ◽  
Calf Thymus ◽  
Thymus Tissue ◽  
Scale Preparation ◽  
Concentrated Solution

Isolation of deoxyribonucleate from a concentrated solution of thymonucleoprotein has been achieved by disruption of the protein nucleate bond with potassium thiocyanate, adsorption of the protein on celite, and alcohol precipitation of the deoxyribonucleate from aqueous salt solution. Highly polymerized nucleate can be obtained readily from 1 lb of calf thymus tissue in high yield.

Cell-Free Protein Synthesis in the Rabbit Liver Ribosomal System. II. Large Scale Preparation of Purified 80S Ribosomes

1975 ◽  
Vol 53 (5) ◽  
pp. 485-494 ◽  
Author(s):  
M. J. Dufresne ◽  
S. J. Igarashi
Keyword(s):  
Large Scale ◽  
Dextran Sulfate ◽  
Deae Cellulose ◽  
Trna Synthetase ◽  
Biologically Active ◽  
Rabbit Liver ◽  
Transferase Activity ◽  
Large Scale Preparation ◽  
Scale Preparation ◽  
Cell Free Protein Synthesis

A procedure for the preparation of a large quantity of biologically active, highly purified ribosomes from rabbit liver is described. The method employs polyethylene glycol – dextran sulfate partition and DEAE-cellulose chromatography to overcome the limitations encountered in conventional procedures. The entire process takes only 48 h to obtain 10 000 A260 units of ribosomes. The ribosomes thus obtained are predominantly 78 S particles with a constant protein–RNA ratio of 0.95. The ribosomes are free from RNase, amino-acyl-tRNA synthetase, and amino-acyl-tRNA:protein transferase activity. The protein synthesizing activity is dependent on added mRNA and protein factors. These ribosomes are stable for prolonged periods of storage in a liquid nitrogen refrigerator.

Purification of the Antihemophilic Factor by Gel Filtration on Agarose

1969 ◽  
Vol 22 (03) ◽  
pp. 577-583 ◽  
Author(s):  
M.M.P Paulssen ◽  
A.C.M.G.B Wouterlood ◽  
H.L.M.A Scheffers
Keyword(s):  
Factor Viii ◽  
Plasma Proteins ◽  
Large Scale ◽  
Gel Filtration ◽  
Large Scale Preparation ◽  
Scale Preparation ◽  
Antihemophilic Factor

SummaryFactor VIII can be isolated from plasma proteins, including fibrinogen by chromatography on agarose. The best results were obtained with Sepharose 6B. Large scale preparation is also possible when cryoprecipitate is separated by chromatography. In most fractions containing factor VIII a turbidity is observed which may be due to the presence of chylomicrons.The purified factor VIII was active in vivo as well as in vitro.

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