دورية أكاديمية
Production and characterization of guinea pig IL-5 in baculovirus-infected insect cells.
| العنوان: | Production and characterization of guinea pig IL-5 in baculovirus-infected insect cells. |
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| المؤلفون: | Mansour M; Department of Molecular Sciences, Pfizer Central Research Division, Groton, Connecticut 06340, USA., Karmilowicz M, Hawrylik SJ, Nalcerio B, Angilly J, Conklyn MJ, Lilly CM, Drazen JM, Lee SE, Auperin DD, De Wet JR, Cohan VL, Showell HJ, Danley DE |
| المصدر: | The American journal of physiology [Am J Physiol] 1996 Jun; Vol. 270 (6 Pt 1), pp. L1002-7. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Physiological Society Country of Publication: United States NLM ID: 0370511 Publication Model: Print Cited Medium: Print ISSN: 0002-9513 (Print) Linking ISSN: 00029513 NLM ISO Abbreviation: Am J Physiol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Bethesda, MD : American Physiological Society Original Publication: Washington [etc.] American Physiological Society. |
| مواضيع طبية MeSH: | Baculoviridae*, Insecta/*virology , Interleukin-5/*genetics, Animals ; Base Sequence ; Cell Line ; Cloning, Molecular ; Guinea Pigs ; Humans ; Interleukin-5/isolation & purification ; Interleukin-5/physiology ; Male ; Mice ; Molecular Sequence Data ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Sequence Homology, Amino Acid |
| مستخلص: | To study the role interleukin (IL)-5 may play in altering airway function in asthma, we have produced recombinant protein for exogenous administration to guinea pigs. The guinea pig IL-5 (gpIL-5) cDNA was cloned by polymerase chain reaction (PCR) amplification of guinea pig spleen RNA and expressed as a secretion product from recombinant baculovirus-infected Sf9 insect cell cultures. The protein was purified to homogeneity by a four-step procedure that included immunoaffinity chromatography using polyclonal antipeptide antibodies against a region of the mature secreted cytokine. The cytokine was properly processed after the signal sequence by the Sf9 cells, was glycosylated with terminal mannose-containing oligosaccharide, and had proper disulfide-linked dimer structure as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified preparation was active in vitro and in vivo as determined by its ability to prime human basophils to release leukotriene C4 in the presence of C5a and to induce airway eosinophilia in naive guinea pigs. |
| سلسلة جزيئية: | GENBANK U34588 |
| المشرفين على المادة: | 0 (Interleukin-5) 0 (Recombinant Proteins) |
| تواريخ الأحداث: | Date Created: 19960601 Date Completed: 19960926 Latest Revision: 20171213 |
| رمز التحديث: | 20240627 |
| DOI: | 10.1152/ajplung.1996.270.6.L1002 |
| PMID: | 8764226 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0002-9513 |
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| DOI: | 10.1152/ajplung.1996.270.6.L1002 |