Expression of biologically active, mature human granulocyte-macrophage colony stimulating factor with an E. coli secretory expression system
Human granulocyte-macrophage colony stimulating factor (HuGM-CSF) was expressed periplasmically in Escherichia coli with the secretory vector, pINIIIompA2. HuGM-CSF protein thus expressed was shown to be faithfully cleaved and biologically active. This protein, however, could not be released by osmo...
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| Veröffentlicht in: | Current microbiology 1988-11, Vol.17 (6), p.321-332 |
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| container_issue | 6 |
| container_start_page | 321 |
| container_title | Current microbiology |
| container_volume | 17 |
| creator | GREENBERG, R LUNDELL, D NARULA, S. K KASTELEIN, R VAN KIMMENADE, A ALROY, Y BONITZ, S CONDON, R FOSSETTA, J FROMMER, B GEWAIN, K KATZ, M LEIBOWITZ, P. J |
| description | Human granulocyte-macrophage colony stimulating factor (HuGM-CSF) was expressed periplasmically in Escherichia coli with the secretory vector, pINIIIompA2. HuGM-CSF protein thus expressed was shown to be faithfully cleaved and biologically active. This protein, however, could not be released by osmotic shock and, on subcellular fractionation, co-sedimented with the outer membrane fraction. The effect of promoters, vectors, host strains, induction conditions and media formulation on expression levels was also evaluated. Some of these factors play a significant role in determining maximal achievable levels of HuGM-CSF in the secretory expression system of E. coli . |
| doi_str_mv | 10.1007/BF01570872 |
| format | Article |
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K ; KASTELEIN, R ; VAN KIMMENADE, A ; ALROY, Y ; BONITZ, S ; CONDON, R ; FOSSETTA, J ; FROMMER, B ; GEWAIN, K ; KATZ, M ; LEIBOWITZ, P. J</creator><creatorcontrib>GREENBERG, R ; LUNDELL, D ; NARULA, S. K ; KASTELEIN, R ; VAN KIMMENADE, A ; ALROY, Y ; BONITZ, S ; CONDON, R ; FOSSETTA, J ; FROMMER, B ; GEWAIN, K ; KATZ, M ; LEIBOWITZ, P. J</creatorcontrib><description>Human granulocyte-macrophage colony stimulating factor (HuGM-CSF) was expressed periplasmically in Escherichia coli with the secretory vector, pINIIIompA2. HuGM-CSF protein thus expressed was shown to be faithfully cleaved and biologically active. This protein, however, could not be released by osmotic shock and, on subcellular fractionation, co-sedimented with the outer membrane fraction. The effect of promoters, vectors, host strains, induction conditions and media formulation on expression levels was also evaluated. Some of these factors play a significant role in determining maximal achievable levels of HuGM-CSF in the secretory expression system of E. coli .</description><identifier>ISSN: 0343-8651</identifier><identifier>EISSN: 1432-0991</identifier><identifier>DOI: 10.1007/BF01570872</identifier><identifier>CODEN: CUMIDD</identifier><language>eng</language><publisher>New York, NY: Springer</publisher><subject>Biological and medical sciences ; Biotechnology ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Health. Pharmaceutical industry ; Industrial applications and implications. 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This protein, however, could not be released by osmotic shock and, on subcellular fractionation, co-sedimented with the outer membrane fraction. The effect of promoters, vectors, host strains, induction conditions and media formulation on expression levels was also evaluated. Some of these factors play a significant role in determining maximal achievable levels of HuGM-CSF in the secretory expression system of E. coli .</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Health. Pharmaceutical industry</subject><subject>Industrial applications and implications. 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K</au><au>KASTELEIN, R</au><au>VAN KIMMENADE, A</au><au>ALROY, Y</au><au>BONITZ, S</au><au>CONDON, R</au><au>FOSSETTA, J</au><au>FROMMER, B</au><au>GEWAIN, K</au><au>KATZ, M</au><au>LEIBOWITZ, P. J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression of biologically active, mature human granulocyte-macrophage colony stimulating factor with an E. coli secretory expression system</atitle><jtitle>Current microbiology</jtitle><date>1988-11</date><risdate>1988</risdate><volume>17</volume><issue>6</issue><spage>321</spage><epage>332</epage><pages>321-332</pages><issn>0343-8651</issn><eissn>1432-0991</eissn><coden>CUMIDD</coden><abstract>Human granulocyte-macrophage colony stimulating factor (HuGM-CSF) was expressed periplasmically in Escherichia coli with the secretory vector, pINIIIompA2. HuGM-CSF protein thus expressed was shown to be faithfully cleaved and biologically active. This protein, however, could not be released by osmotic shock and, on subcellular fractionation, co-sedimented with the outer membrane fraction. The effect of promoters, vectors, host strains, induction conditions and media formulation on expression levels was also evaluated. Some of these factors play a significant role in determining maximal achievable levels of HuGM-CSF in the secretory expression system of E. coli .</abstract><cop>New York, NY</cop><pub>Springer</pub><doi>10.1007/BF01570872</doi><tpages>12</tpages></addata></record> |
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| ispartof | Current microbiology, 1988-11, Vol.17 (6), p.321-332 |
| issn | 0343-8651 1432-0991 |
| language | eng |
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| source | Springer Nature - Complete Springer Journals |
| subjects | Biological and medical sciences Biotechnology Escherichia coli Fundamental and applied biological sciences. Psychology Health. Pharmaceutical industry Industrial applications and implications. Economical aspects Other active biomolecules Production of active biomolecules |
| title | Expression of biologically active, mature human granulocyte-macrophage colony stimulating factor with an E. coli secretory expression system |
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