Controlled expression of human basic fibroblast growth factor mutein CS23 in Escherichia coli under a bacteriophage T7 promoter

Kuriyama, Masato; Nakatu, Masanori; Nakao, Megumi; Igarashi, Koichi; Kitano, Kazuaki

doi:10.1016/0922-338x(92)80002-z

Cited by 10 publications

(1 citation statement)

References 21 publications

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“…In chemically inducible expression systems, it is known that the induction conditions greatly affect the expression of cloned genes. 15 ,19,23) Kuriyama et al 7 ) reported that hbFGF mutein CS23 accumulated in a soluble form under "controlled expression". In their cultivation, the affinity of the repressor protein for the lacUV5 promoter was controlled by changing the concentration of the inducer, IPTG.…”

Section: Discussionmentioning

confidence: 99%

Expression of Aqualysin I (a Thermophilic Protease) in Soluble Form inEscherichia coliunder a Bacteriophage T7 Promoter

Sakamoto

Terada

Iijima

et al. 1995

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionmentioning

confidence: 99%

Expression of Aqualysin I (a Thermophilic Protease) in Soluble Form inEscherichia coliunder a Bacteriophage T7 Promoter

Sakamoto

Terada

Iijima

et al. 1995

Bioscience, Biotechnology, and Biochemistry

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Refolding of therapeutic proteins produced inEscherichia coli as inclusion bodies

1999

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Overexpression of cloned or synthetic genes in Escherichia coli often results in the formation of insoluble protein inclusion bodies. Within the last decade, specific methods and strategies have been developed for preparing active recombinant proteins from these inclusion bodies. Usually, the inclusion bodies can be separated easily from other cell components by centrifugation, solubilized by denaturants such as guanidine hydrochloride (Gdn‐HCl) or urea, and then renatured through a refolding process such as dilution or dialysis. Recent improvements in renaturation procedures have included the inhibition of aggregation during refolding by application of low molecular weight additives and matrix‐bound renaturation. These methods have made it possible to obtain high yields of biologically active proteins by taking into account process parameters such as protein concentration, redox conditions, temperature, pH, and ionic strength. © 1999 John Wiley & Sons, Inc. Biopoly 51: 297–307, 1999

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The kinetics of RCC1 inclusion body formation in Escherichia Coli

Tsai

Betenbaugh

Shiloach

1995

Biotech & Bioengineering

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The Regulator of Chromosome Condensation protein (RCC1) is located in both the soluble and inclusion body (IB) fractions of the whole cell lysate when expressed in Escherichia coli BL21 (pLysS) at temperatures below 30 degrees C. When bacterial growth was carried out at 20 degrees C, the majority of the RCC1 remained soluble up to 5.5 h postinduction, When the temperature was raised to 25 degrees C, RCC1 IB was dominant by 1.5 h postinduction. The shift in RCC1 IB formation with temperature suggests that in addition to increased translation rates, folding and aggregation processes may contribute to RCC1 IB formation at higher temperatures. (c) 1995 John Wiley & Sons, Inc.

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Controlled expression of human basic fibroblast growth factor mutein CS23 in Escherichia coli under a bacteriophage T7 promoter

Cited by 10 publications

References 21 publications

Expression of Aqualysin I (a Thermophilic Protease) in Soluble Form inEscherichia coliunder a Bacteriophage T7 Promoter

Expression of Aqualysin I (a Thermophilic Protease) in Soluble Form inEscherichia coliunder a Bacteriophage T7 Promoter

Refolding of therapeutic proteins produced inEscherichia coli as inclusion bodies

The kinetics of RCC1 inclusion body formation in Escherichia Coli

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