scholarly journals Biochemical characterization of a mutant asparaginyl-tRNA synthetase from Chinese hamster ovary cells.

1978 ◽  
Vol 253 (1) ◽  
pp. 58-62 ◽  
Author(s):  
I.L. Andrulis ◽  
C.S. Chiang ◽  
S.M. Arfin ◽  
T.A. Miner ◽  
G.W. Hatfield
1994 ◽  
Vol 11 (1) ◽  
pp. 43-50 ◽  
Author(s):  
Peter P�hlsson ◽  
Douglas P. Blackall ◽  
Maciej Ugorski ◽  
Marcin Czerwinski ◽  
Steven L. Spitalnik

1984 ◽  
Vol 4 (1) ◽  
pp. 173-180 ◽  
Author(s):  
S W Stanfield ◽  
D R Helinski

Small polydisperse circular (spc) DNA was isolated and cloned, using BglII from Chinese hamster ovary (CHO) cells. The properties of 47 clones containing at least 43 different BglII fragments are reported. The majority of the clones probably contain entire sequences from individual spcDNA molecules. Most of the clones were homologous to sequences in CHO cell chromosomal DNA, and many were also homologous to mouse LMTK- cell chromosomal sequences. The majority of homologous CHO cell chromosomal sequences were repetitive, although a few may be single copy. Only a small fraction of cloned spcDNA molecules were present in every cell; most occurred less frequently than once in 15 cells. Localization studies indicated that at least a portion of spcDNA is associated with the nucleus in CHO cells.


1989 ◽  
Vol 9 (5) ◽  
pp. 1832-1838
Author(s):  
K J Kontis ◽  
S M Arfin

A cDNA for threonyl-tRNA synthetase was isolated from a human placental cDNA lambda gt11 expression library by immunological screening, and its identity was confirmed by hybrid-selected mRNA translation. With this cDNA used as a hybridization probe, borrelidin-resistant Chinese hamster ovary cells that overproduced threonyl-tRNA synthetase were shown to have increased levels of threonyl-tRNA synthetase mRNA and gene sequences. Amplification of the gene did not appear to have been accompanied by any major structural reorganizations.


1984 ◽  
Vol 4 (9) ◽  
pp. 1939-1941
Author(s):  
R E Cirullo ◽  
J J Wasmuth

Temperature-resistant revertants, derived from the temperature-sensitive CHO asparaginyl-tRNA synthetase mutant, Asn-5, were isolated and characterized. Several lines of evidence indicate that the temperature-resistant phenotype of the revertants is due to their overproducing the same altered enzyme present in the Asn-5 parent.


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