Adaptation of an insect cell line (Agallia constricta) in a mammalian cell culture medium

In Vitro ◽  
1973 ◽  
Vol 8 (5) ◽  
pp. 375-378 ◽  
Author(s):  
Arthur H. Intosh ◽  
K. Maramorosch ◽  
C. Rechtoris
Keyword(s):  
Cell Culture ◽  
Cell Line ◽  
Mammalian Cell ◽  
Insect Cell ◽  
Culture Medium ◽  
Mammalian Cell Culture ◽  
Insect Cell Line ◽  
Cell Culture Medium

Development of an Assay for the Measurement of the Surfactant Pluronic F-68 in Mammalian Cell Culture Medium

1998 ◽  
Vol 262 (1) ◽  
pp. 39-44 ◽  
Author(s):  
Hazem Ghebeh ◽  
Anita Handa-Corrigan ◽  
Michael Butler
Keyword(s):  
Cell Culture ◽  
Mammalian Cell ◽  
Culture Medium ◽  
Mammalian Cell Culture ◽  
Cell Culture Medium

Effect of mammalian cell culture medium on the gelation properties of Pluronic® F127

Biomaterials ◽  
2002 ◽  
Vol 23 (23) ◽  
pp. 4615-4619 ◽  
Author(s):  
Julie E Matthew ◽  
Yesenia L Nazario ◽  
Susan C Roberts ◽  
Surita R Bhatia
Keyword(s):  
Cell Culture ◽  
Mammalian Cell ◽  
Culture Medium ◽  
Mammalian Cell Culture ◽  
Cell Culture Medium

scholarly journals Combination of nutrients in a mammalian cell culture medium kills cryptococci

2018 ◽  
Vol 57 (3) ◽  
pp. 374-383 ◽  
Author(s):  
Donald L Granger ◽  
Donna M Call
Keyword(s):  
Cell Culture ◽  
Mammalian Cell ◽  
Culture Medium ◽  
Mammalian Cell Culture ◽  
Cell Culture Medium

scholarly journals Analysis of a Novel Insect Cell Culture Medium-Based Growth Medium for Bartonella Species

2008 ◽  
Vol 74 (16) ◽  
pp. 5224-5227 ◽  
Author(s):  
Tanja Riess ◽  
Florian Dietrich ◽  
Katja V. Schmidt ◽  
Patrick O. Kaiser ◽  
Heinz Schwarz ◽  
...  
Keyword(s):  
Cell Culture ◽  
Insect Cell ◽  
Culture Medium ◽  
Expression Patterns ◽  
Insect Cell Culture ◽  
Host Cells ◽  
Cell Culture Medium ◽  
Bacterial Protein ◽  
Bartonella Species ◽  
Slow Growing

ABSTRACT Human- and animal-pathogenic Bartonella species are fastidious and slow-growing bacteria difficult to isolate and cultivate. We describe a novel, easy-to-prepare liquid medium for the fast and reliable growth of several Bartonella spp. that does not affect bacterial protein expression patterns or interactions with host cells.

High-level expression of recombinant immunoreactive thyroid peroxidase in the High Five insect cell line

1996 ◽  
Vol 17 (2) ◽  
pp. 165-174 ◽  
Author(s):  
F Grennan Jones ◽  
A Wolstenholme ◽  
S Fowler ◽  
S Smith ◽  
K Ziemnicka ◽  
...  
Keyword(s):  
Cell Line ◽  
Cell Lines ◽  
Insect Cell ◽  
Culture Medium ◽  
Aminolevulinic Acid ◽  
Expression System ◽  
Insect Cell Line ◽  
Thyroid Peroxidase ◽  
High Five Cells ◽  
Insect Cell Lines

ABSTRACT Expression of a major thyroid autoantigen, thyroid peroxidase (TPO) was studied using the baculovirus-insect cell expression system. Human TPO cDNA modified so as to code for the extracellular fragment of the protein was placed under the control of the strong polyhedrin promoter in baculovirus transfer vector pBlueBacIII and cotransfected with linearized AcMNPV viral DNA. Expression in two insect cell lines Spodoptera frugiperda (Sf9) and Tricoplusia ni (High Five) was investigated and levels of recombinant TPO (rTPO) monitored by RIA and SDS-PAGE followed by Western blotting. Both insect cell lines expressed rTPO, but higher levels (30 mg/l culture medium) were obtained with High Five cells. Culture medium rTPO was purified and its glycosylation and immunoreactivity analysed. Lectin-affinity blotting and treatment with glycosidases indicated that both high mannose and complex-type sugar residues were associated with the recombinant protein. Studies with an ELISA based on biotin-labelled rTPO and an immunoprecipitation assay based on 125I-labelled rTPO indicated that the rTPO and native TPO showed similar reactivity to TPO autoantibodies (r=0·96, P<0·001, n=50 and r=0·99, P<0·001, n=80 respectively). In addition, rTPO expressed in High Five cells showed enzyme activity comparable with that of native TPO when the heme biosynthesis precursor δ-aminolevulinic acid was included in the culture medium. Overall, our studies indicate that the High Five insect cell line provides a useful system for the expression of relatively high levels of rTPO which should be suitable for structural analysis of TPO and TPO—TPO autoantibody complexes.

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