Inhibition of serine palmitoyltransferase in vitro and long-chain base biosynthesis in intact Chinese hamster ovary cells by .beta.-chloroalanine

Biochemistry ◽  
1988 ◽  
Vol 27 (18) ◽  
pp. 7079-7084 ◽  
Author(s):  
Kimberly A. Medlock ◽  
Alfred H. Merrill
Keyword(s):  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Serine Palmitoyltransferase ◽  
Ovary Cells ◽  
Chain Base ◽  
Long Chain Base ◽  
Long Chain

Persistence of sister chromatid exchange by 9-β-D-arabinofuranosyladenine in Chinese hamster ovary cells cultivated in vitro

Mutagenesis ◽  
1993 ◽  
Vol 8 (5) ◽  
pp. 445-448 ◽  
Author(s):  
Paolo Perticone ◽  
Marco Linguardo ◽  
Renata Cozzi ◽  
Rosa Maria Corbo ◽  
Stefania Polani
Keyword(s):  
Sister Chromatid ◽  
Chinese Hamster Ovary ◽  
Sister Chromatid Exchange ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Ovary Cells

In vitro biosynthesis of diphthamide, studied with mutant Chinese hamster ovary cells resistant to diphtheria toxin

1984 ◽  
Vol 4 (4) ◽  
pp. 642-650
Author(s):  
T J Moehring ◽  
D E Danley ◽  
J M Moehring
Keyword(s):  
Chinese Hamster Ovary ◽  
Diphtheria Toxin ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Elongation Factor ◽  
Synthetase Activity ◽  
Post Translational Modification ◽  
Ovary Cells ◽  
Elongation Factor 2

Diphthamide, a unique amino acid, is a post-translational derivative of histidine that exists in protein synthesis elongation factor 2 at the site of diphtheria toxin-catalyzed ADP-ribosylation of elongation factor 2. We investigated steps in the biosynthesis of diphthamide with mutants of Chinese hamster ovary cells that were altered in different steps of this complex post-translational modification. Biochemical evidence indicates that this modification requires a minimum of three steps, two of which we accomplished in vitro. We identified a methyltransferase activity that transfers methyl groups from S-adenosyl methionine to an unmethylated form of diphthine (the deamidated form of diphthamide), and we tentatively identified an ATP-dependent synthetase activity involved in the biosynthesis of diphthamide from diphthine. Our results are in accord with the proposed structure of diphthamide (B. G. VanNess, et al., J. Biol. Chem. 255:10710-10716, 1980).

scholarly journals Novel Promoters Derived from Chinese Hamster Ovary Cells via In Silico and In Vitro Analysis

2019 ◽  
Vol 14 (11) ◽  
pp. 1900125 ◽  
Author(s):  
Ly N. Nguyen ◽  
Martina Baumann ◽  
Heena Dhiman ◽  
Nicolas Marx ◽  
Valerie Schmieder ◽  
...  
Keyword(s):  
Chinese Hamster Ovary ◽  
In Silico ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Ovary Cells ◽  
Vitro Analysis ◽  
In Vitro Analysis

scholarly journals Properties of the kinetochore in vitro. I. Microtubule nucleation and tubulin binding.

1985 ◽  
Vol 101 (3) ◽  
pp. 755-765 ◽  
Author(s):  
T J Mitchison ◽  
M W Kirschner
Keyword(s):  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Lag Phase ◽  
Ovary Cells ◽  
Tubulin Binding ◽  
Mixed Polarity ◽  
Tubulin Immunofluorescence

We have isolated chromosomes from Chinese hamster ovary cells arrested in mitosis with vinblastine and examined the interactions of their kinetochores with purified tubulin in vitro. The kinetochores nucleate microtubule (MT) growth with complex kinetics. After an initial lag phase, MTs are continuously nucleated with both plus and minus ends distally localized. This mixed polarity seems inconsistent with the formation of an ordered, homopolar kinetochore fiber in vivo. As isolated from vinblastine-arrested cells, kinetochores contain no bound tubulin. The kinetochores of chromosomes isolated from colcemid-arrested cells or of chromosomes incubated with tubulin in vitro are brightly stained after anti-tubulin immunofluorescence. This bound tubulin is probably not in the form of MTs. It is localized to the corona region by immunoelectron microscopy, where it may play a role in MT nucleation in vitro.

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