Factors affecting the synthesis of the n-terminal methionine-free molecule of recombinant human interleukin-2 by Escherichia coli

Fujimoto, Shigeru; Nakatsu, Masanori; Kato, Koichi; Kitano, Kazuaki

doi:10.1016/0385-6380(88)90045-3

Cited by 8 publications

(2 citation statements)

References 16 publications

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“…1). This sequence thus revealed the loss of the N-terminal methionine, which was also observed in other recombinant proteins expressed in E. coli, such as human pro-urokinase and human interleukin-2 [16,17]. Although the N-terminal methionine is lost with the first two residues (Ile-Thr) left unidentified, the rest of the sequence was found to be totally identical to the intracellular enzyme ( Table 2).…”

Section: Determination Of Amino Acid Sequence Of the Proteinsupporting

confidence: 62%

Purification and characterization of the recombinant alginate lyase from Pseudomonas sp. leaked by Escherichia coli upon addition of glycine

Fujiyama¹

1995

FEMS Microbiology Letters

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The plasmid pAL205 encodes an alginate lyase gene of Pseudomonas sp. OS-ALG-9, fused in frame to the beta-galactosidase alpha-peptide gene. The alginate lyase (Aly) expressed in Escherichia coli (pAL205) was significantly secreted into the medium by the addition of glycine. The extracellular enzyme isolated from the culture of E. coli JM109 (pAL205) was purified over 15,000-fold by successive chromatography and subjected to amino acid sequence analysis. The sequence determined was identical to that of the intracellular protein. Since the activity and molecular size of the extracellular Aly is identical to the intracellular protein and to the Aly isolated from Pseudomonas, the glycine does not affect or modify the Aly during its leakage into the medium.

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Section: Determination Of Amino Acid Sequence Of the Proteinsupporting

confidence: 62%

Purification and characterization of the recombinant alginate lyase from Pseudomonas sp. leaked by Escherichia coli upon addition of glycine

Fujiyama¹

1995

FEMS Microbiology Letters

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“…Ham's F12 medium was produced by Nissui Seiyaku Co. Insulin and transferrin were from the Sigma Co. Ethanolamine, Sodium selenite and PEG 20,000 were from Wako Pure Chemical Co. FCS was from Armour Pharmaceutical Co. GFS was prepared at our Hikari Plant. Human recombinant IL-2 with specific activity of 3.0 x 10 4 U/mg was prepared in our Laboratory (Fujimoto et al, 1988).…”

Section: Chemicalsmentioning

confidence: 99%

Improvement in the antibody productivity of human-human hybridomas by transfection with Tac gene

et al. 1990

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The presence of a highly purified recombinant interleukin-2 (rIL-2) increased the production of immunoglobulin (IgM or IgG) by human-human hybridomas to 1.5-2.0 times the production by untreated cells. However, these cells did not react with anti-Tac (IL-2 receptor alpha) antibody. To enhance the response of the hybridoma cells to rIL-2, Tac gene was introduced by co-transfection with Tac gene expression plasmid pTB459 and G418 resistant gene expression plasmid pRSVneo. Tac cDNA transfected hybridoma (HBW-4.16.459-6-126) was induced to produce 6 times as much IgG by rIL-2 as was the control. This antibody production promoting phenomenon mediated by rIL-2 was depressed by anti-Tac antibody.

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Expression in Escherichia coli of rat liver cytosolic glutathione S-transferase Yc cDNA

Huskey

Wang

Linemeyer

et al. 1990

Archives of Biochemistry and Biophysics

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Factors affecting the synthesis of the n-terminal methionine-free molecule of recombinant human interleukin-2 by Escherichia coli

Cited by 8 publications

References 16 publications

Purification and characterization of the recombinant alginate lyase from Pseudomonas sp. leaked by Escherichia coli upon addition of glycine

Purification and characterization of the recombinant alginate lyase from Pseudomonas sp. leaked by Escherichia coli upon addition of glycine

Improvement in the antibody productivity of human-human hybridomas by transfection with Tac gene

Expression in Escherichia coli of rat liver cytosolic glutathione S-transferase Yc cDNA

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