scholarly journals DNA-dependent RNA polymerase III from Acanthamoeba castellanii. A rapid procedure for the large scale preparation of homogeneous enzyme.

1978 ◽  
Vol 253 (17) ◽  
pp. 6242-6248
Author(s):  
S.R. Spindler ◽  
J.M. D'Alessio ◽  
G.L. Duester ◽  
M.R. Paule
Keyword(s):  
Rna Polymerase ◽  
Large Scale ◽  
Rna Polymerase Iii ◽  
Acanthamoeba Castellanii ◽  
Rapid Procedure ◽  
Polymerase Iii ◽  
Large Scale Preparation ◽  
Scale Preparation

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.

scholarly journals A cancer-associated RNA polymerase III identity drives robust transcription and expression of SNAR-A noncoding RNA

2021 ◽  
Author(s):  
Kevin Van Bortle ◽  
David P. Marciano ◽  
Qing Liu ◽  
Andrew M. Lipchik ◽  
Sanjay Gollapudi ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Noncoding Rna ◽  
Large Scale ◽  
Immune Cell ◽  
Rna Polymerase Iii ◽  
Specific Class ◽  
Proliferating Cells ◽  
Small Noncoding Rna ◽  
Polymerase Iii ◽  
Pol Iii

ABSTRACTDysregulation of the RNA polymerase III (Pol III) transcription program, which synthesizes tRNA and other classes of small noncoding RNA critical for cell growth and proliferation, is associated with cancer and human disease. Previous studies have identified two distinct Pol III isoforms defined by the incorporation of either subunit POLR3G (RPC7α) during early development, or POLR3GL (RPC7β) in specialized tissues. Though POLR3G is re-established in cancer and immortalized cell lines, the contributions of these isoforms to transcription potential and transcription dysregulation in cancer remain poorly defined. Using an integrated Pol III genomic profiling approach in combination with in vitro differentiation and subunit disruption experiments, we discover that loss of subunit POLR3G is accompanied by a restricted repertoire of genes transcribed by Pol III. In particular, we observe that a specific class of small noncoding RNA, SNAR-A, is exquisitely sensitive to the availability of subunit POLR3G in proliferating cells. Taken further, large-scale analysis of Pol III subunit expression and downstream chromatin features identifies concomitant loss of POLR3G and SNAR-A activity across a multitude of differentiated primary immune cell lineages, and conversely, coordinate re-establishment of POLR3G expression and SNAR-A features in a variety of human cancers. These results altogether argue against strict redundancy models for subunits POLR3G and POLR3GL, and instead support a model in which Pol III identity itself functions as an important transcriptional regulatory mechanism. Upregulation of POLR3G, which is driven by MYC, identifies a subgroup of patients with unfavorable survival outcomes in specific cancers, further implicating the POLR3G-enhanced transcription repertoire as a potential disease factor.

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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