{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T08:50:39Z","timestamp":1790326239606,"version":"4.1.0"},"reference-count":35,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2004,10,1]],"date-time":"2004-10-01T00:00:00Z","timestamp":1096588800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Expression and Purification"],"published-print":{"date-parts":[[2004,10]]},"DOI":"10.1016\/j.pep.2004.06.022","type":"journal-article","created":{"date-parts":[[2004,7,30]],"date-time":"2004-07-30T05:37:42Z","timestamp":1091165862000},"page":"399-408","source":"Crossref","is-referenced-by-count":37,"title":["Production and purification of a chimeric monoclonal antibody against botulinum neurotoxin serotype A"],"prefix":"10.1016","volume":"37","author":[{"given":"Mark C.","family":"Mowry","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mike","family":"Meagher","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leonard","family":"Smith","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jim","family":"Marks","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anu","family":"Subramanian","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.pep.2004.06.022_bib1","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1038\/nbt0901-819","article-title":"Monoclonal antibodies in the clinic","volume":"19","author":"Reichert","year":"2001","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.pep.2004.06.022_bib2","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/417584a","article-title":"Therapeutic antibodies: magic bullets hit the target","volume":"417","author":"Gura","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.pep.2004.06.022_bib3","doi-asserted-by":"crossref","first-page":"11346","DOI":"10.1073\/pnas.172229899","article-title":"Potent neutralization of botulinum neurotoxin by recombinant oligoclonal antibody","volume":"99","author":"Nowakowski","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.pep.2004.06.022_bib4","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1001\/jama.285.8.1059","article-title":"Botulinum toxin as a biological weapon: medical and public health management","volume":"285","author":"Arnon","year":"2001","journal-title":"JAMA"},{"key":"10.1016\/j.pep.2004.06.022_bib5","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1006\/jmbi.1999.2945","article-title":"Sequence homology and structural analysis of the clostridial neurotoxins","volume":"291","author":"Lacy","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.pep.2004.06.022_bib6","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1054\/jocn.2000.0684","article-title":"The current use of botulinum toxin","volume":"7","author":"Mahant","year":"2000","journal-title":"J. Clin. Neurosci."},{"key":"10.1016\/j.pep.2004.06.022_bib7","doi-asserted-by":"crossref","first-page":"2351","DOI":"10.1128\/JCM.26.11.2351-2356.1988","article-title":"Human immune response to botulinum pentavalent (ABCDE) toxoid determined by a neutralization test and by an enzyme-linked immunosorbent assay","volume":"26","author":"Siegel","year":"1988","journal-title":"J. Clin. Microbiol."},{"key":"10.1016\/j.pep.2004.06.022_bib8","doi-asserted-by":"crossref","first-page":"955","DOI":"10.1016\/S0300-9084(00)01173-1","article-title":"Development of vaccines for prevention of botulism","volume":"82","author":"Byrne","year":"2000","journal-title":"Biochimie"},{"key":"10.1016\/j.pep.2004.06.022_bib9","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1093\/clinids\/23.2.337","article-title":"Experience with the use of an investigational F(ab\u2032)2 heptavalent botulism immune globulin of equine origin during an outbreak of type E botulism in Egypt","volume":"23","author":"Hibbs","year":"1996","journal-title":"Clin. Infect. Dis."},{"issue":"Suppl. 1","key":"10.1016\/j.pep.2004.06.022_bib10","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1002\/(SICI)1099-1263(199912)19:1+<S35::AID-JAT612>3.0.CO;2-9","article-title":"Protection against botulinum toxins provided by passive immunization with botulinum human immune globulin: evaluation using an inhalation model","volume":"19","author":"Gelzleichter","year":"1999","journal-title":"J. Appl. Toxicol."},{"key":"10.1016\/j.pep.2004.06.022_bib11","doi-asserted-by":"crossref","first-page":"4216","DOI":"10.1073\/pnas.77.7.4216","article-title":"Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity","volume":"77","author":"Urlaub","year":"1980","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.pep.2004.06.022_bib12","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1016\/S0021-9258(17)34875-5","article-title":"Selective multiplication of dihydrofolate reductase genes in methotrexate-resistant variants of cultured murine cells","volume":"253","author":"Alt","year":"1978","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.pep.2004.06.022_bib13","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1128\/MCB.3.4.699","article-title":"Evolution of chromosomal regions containing transfected and amplified dihydrofolate reductase sequences","volume":"3","author":"Kaufman","year":"1983","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.pep.2004.06.022_bib14","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1002\/(SICI)1097-0290(19981220)60:6<679::AID-BIT5>3.0.CO;2-Q","article-title":"Clonal variability within dihydrofolate reductase-mediated gene amplified Chinese hamster ovary cells: stability in the absence of selective pressure","volume":"60","author":"Kim","year":"1998","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.pep.2004.06.022_bib15","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1021\/bp000114e","article-title":"Amplified gene location in chromosomal DNA affected recombinant protein production and stability of amplified genes","volume":"16","author":"Yoshikawa","year":"2000","journal-title":"Biotechnol. Prog."},{"key":"10.1016\/j.pep.2004.06.022_bib16","first-page":"119","article-title":"Effect of cloned gene dosage on cell growth and hepatitis B surface antigen synthesis and secretion in recombinant CHO cells","volume":"40","author":"Pendse","year":"1992","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.pep.2004.06.022_bib17","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1038\/nbt0191-64","article-title":"High level expression of the humanized monoclonal antibody Campath-1H in Chinese hamster ovary cell","volume":"9","author":"Page","year":"1991","journal-title":"Bio\/Technology"},{"key":"10.1016\/j.pep.2004.06.022_bib18","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/0022-1759(78)90259-4","article-title":"Use of staphylococcal protein A as an immunological reagent","volume":"20","author":"Goding","year":"1978","journal-title":"J. Immunol. Methods"},{"key":"10.1016\/j.pep.2004.06.022_bib19","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0022-1759(83)90104-7","article-title":"Binding of immunoglobulins to protein A and immunoglobulin levels in mammalian sera","volume":"62","author":"Lindmark","year":"1983","journal-title":"J. Immunol. Methods"},{"key":"10.1016\/j.pep.2004.06.022_bib20","first-page":"309","article-title":"Quantitative binding studies of a monoclonal antibody to immobilized protein-A","volume":"2","author":"Biedermann","year":"1991","journal-title":"Bioseparation"},{"key":"10.1016\/j.pep.2004.06.022_bib21","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/0022-1759(93)90013-W","article-title":"Assessment of the suitability of commercially available SpA affinity solid phases for the purification of murine monoclonal antibodies at process scale","volume":"160","author":"Godfrey","year":"1993","journal-title":"J. Immunol. Methods"},{"key":"10.1016\/j.pep.2004.06.022_bib22","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1002\/jmr.300080116","article-title":"Optimization of protein G chromatography for biopharmaceutical monoclonal antibodies","volume":"8","author":"Bill","year":"1995","journal-title":"J. Mol. Recognit."},{"key":"10.1016\/j.pep.2004.06.022_bib23","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/BF00754610","article-title":"Production of mouse monoclonal antibodies using a continuous cell culture fermenter and protein G affinity chromatography","volume":"16","author":"Zamboni","year":"1994","journal-title":"Cytotechnology"},{"key":"10.1016\/j.pep.2004.06.022_bib24","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/0165-022X(93)90005-9","article-title":"Purification of monoclonal antibodies with light-chain heterogeneity produced by mouse hybridomas raised with NS-1 myelomas: application of hydrophobic interaction high-performance liquid chromatography","volume":"27","author":"Abe","year":"1993","journal-title":"J. Biochem. Biophys. Methods"},{"key":"10.1016\/j.pep.2004.06.022_bib25","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S0022-1759(97)00129-4","article-title":"Single-step purification of bispecific monoclonal antibodies for immunotherapeutic use by hydrophobic interaction chromatography","volume":"208","author":"Manzke","year":"1997","journal-title":"J. Immunol. Methods"},{"key":"10.1016\/j.pep.2004.06.022_bib26","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/0003-2697(89)90088-2","article-title":"A thiophilic adsorbent for the one-step high-performance liquid chromatography purification of monoclonal antibodies","volume":"180","author":"Nopper","year":"1989","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.pep.2004.06.022_bib27","first-page":"7","article-title":"Ion exchange resins for the purification of monoclonal antibodies from animal cell culture","volume":"4","author":"Graf","year":"1994","journal-title":"Bioseparation"},{"key":"10.1016\/j.pep.2004.06.022_bib28","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0021-9673(98)00999-6","article-title":"Purification of monoclonal antibodies from cell culture supernatants using a modified zirconia based cation-exchange support","volume":"831","author":"Clausen","year":"1999","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.pep.2004.06.022_bib29","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/S0021-9673(00)00289-2","article-title":"Use of spray-dried zirconia microspheres in the separation of immunoglobulins from cell culture supernatant","volume":"890","author":"Subramanian","year":"2000","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.pep.2004.06.022_bib30","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/0021-9673(93)80284-F","article-title":"Chemistry of zirconia and its use in chromatography","volume":"657","author":"Nawrocki","year":"1993","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.pep.2004.06.022_bib31","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/S0021-9673(00)01013-X","article-title":"Comparison of hydrophobic charge induction chromatography with affinity chromatography on protein A for harvest and purification of antibodies","volume":"908","author":"Schwartz","year":"2001","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.pep.2004.06.022_bib32","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/S0021-9673(98)00436-1","article-title":"Hydrophobic charge induction chromatography: salt independent protein adsorption and facile elution with aqueous buffers","volume":"814","author":"Burton","year":"1998","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.pep.2004.06.022_bib33","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1042\/BA20000090","article-title":"Chromosome localization and gene-copy-number quantification of three random integrations in Chinese-hamster ovary cells and their amplified cell lines using fluorescence in situ hybridization","volume":"33","author":"Davies","year":"2001","journal-title":"Biotechnol. Appl. Biochem."},{"key":"10.1016\/j.pep.2004.06.022_bib34","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1046\/j.1538-7836.2003.00153.x","article-title":"A monoclonal antibody against activated protein C allows rapid detection of activated protein C in plasma and reveals a calcium ion dependent epitope involved in factor Va inactivation","volume":"1","author":"Liaw","year":"2003","journal-title":"J. Thromb. Haemost."},{"key":"10.1016\/j.pep.2004.06.022_bib35","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1006\/abio.2000.4919","article-title":"Biosensor-based estimation of kinetic and equilibrium constants","volume":"290","author":"Quinn","year":"2001","journal-title":"Anal. Biochem."}],"container-title":["Protein Expression and Purification"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1046592804002311?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1046592804002311?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,24]],"date-time":"2021-06-24T18:03:37Z","timestamp":1624557817000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1046592804002311"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,10]]},"references-count":35,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2004,10]]}},"alternative-id":["S1046592804002311"],"URL":"https:\/\/doi.org\/10.1016\/j.pep.2004.06.022","relation":{},"ISSN":["1046-5928"],"issn-type":[{"value":"1046-5928","type":"print"}],"subject":[],"published":{"date-parts":[[2004,10]]}}}