{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T05:51:20Z","timestamp":1790920280331,"version":"4.1.0"},"reference-count":27,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2011,12,28]],"date-time":"2011-12-28T00:00:00Z","timestamp":1325030400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100002241","name":"Japan Science and Technology Agency","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002241","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003382","name":"Core Research for Evolutional Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003382","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2012,4]]},"abstract":"<jats:p>\n                    The ultimate goal of catalytic antibody research is to develop new patient therapies that use the advantages offered by human catalytic antibodies. The establishment of a high\u2010throughput method for obtaining valuable candidate catalytic antibodies must be accelerated to achieve this objective. In this study, based on our concept that we can find antibody light chains with a high probability of success if they include a serine protease\u2010like catalytic triad composed of Ser, His, and Asp on a variable region of the antibody structure, we amplified and cloned DNAs encoding human antibody light chains from germline genes of subgroup II by seminested PCR using two primer sets designed for this purpose. Seven DNA fragments encoding light chains in 17 clones were derived from germline gene A18b, 6 DNA fragments from A3\/A19, 2 DNA fragments from A17, and a clone DNA fragment from A5 and O11\/O1. All light chains expressed in\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    and highly purified under nondenaturing conditions exhibited amidolytic activity against synthetic peptides. Some of the light chains exhibited unique features that suppressed the infectious activity of the rabies virus. Furthermore, the survival rate of mice in which a lethal level of the rabies virus was coinoculated directly into the brain with light chain 18 was significantly improved. In the case of humans, these results demonstrate that high\u2010throughput selection of light chains possessing catalytic functions and specificity for a target molecule can be attained from a light\u2010chain DNA library amplified from germline genes belonging to subgroup II.\u2014Hifumi, E., Honjo, E., Fujimoto, N., Arakawa, M., Nishizono, A., Uda, T. Highly efficient method of preparing human catalytic antibody light chains and their biological characteristics.\n                    <jats:italic>FASEB J.<\/jats:italic>\n                    26, 1607\u20131615 (2012).\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.fasebj.org\">www.fasebj.org<\/jats:ext-link>\n                  <\/jats:p>","DOI":"10.1096\/fj.11-195339","type":"journal-article","created":{"date-parts":[[2011,12,28]],"date-time":"2011-12-28T22:30:57Z","timestamp":1325111457000},"page":"1607-1615","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":33,"title":["Highly efficient method of preparing human catalytic antibody light chains and their biological characteristics"],"prefix":"10.1096","volume":"26","author":[{"given":"Emi","family":"Hifumi","sequence":"first","affiliation":[{"name":"Research Center for Applied Medical Engineering Faculty of Engineering Oita University Oita Japan"},{"name":"Japan Science and Technology Agency\u2010Core Research for Evolutional Science and Technology (JST\u2010CREST) Kawaguchi Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eijiro","family":"Honjo","sequence":"additional","affiliation":[{"name":"Department of Applied Chemistry Faculty of Engineering Oita University Oita Japan"},{"name":"Japan Science and Technology Agency\u2010Core Research for Evolutional Science and Technology (JST\u2010CREST) Kawaguchi Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naoko","family":"Fujimoto","sequence":"additional","affiliation":[{"name":"Department of Applied Chemistry Faculty of Engineering Oita University Oita Japan"},{"name":"Japan Science and Technology Agency\u2010Core Research for Evolutional Science and Technology (JST\u2010CREST) Kawaguchi Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mitsue","family":"Arakawa","sequence":"additional","affiliation":[{"name":"Department of Nursing Faculty of Medicine Oita University Yufu Japan"},{"name":"Japan Science and Technology Agency\u2010Core Research for Evolutional Science and Technology (JST\u2010CREST) Kawaguchi Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akira","family":"Nishizono","sequence":"additional","affiliation":[{"name":"Department of Microbiology Faculty of Medicine Oita University Yufu Japan"},{"name":"Japan Science and Technology Agency\u2010Core Research for Evolutional Science and Technology (JST\u2010CREST) Kawaguchi Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Taizo","family":"Uda","sequence":"additional","affiliation":[{"name":"Department of Applied Chemistry Faculty of Engineering Oita University Oita Japan"},{"name":"Japan Science and Technology Agency\u2010Core Research for Evolutional Science and Technology (JST\u2010CREST) Kawaguchi Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2011,12,28]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.2024118"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)98440-1"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1585181"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-1759(02)00242-9"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M406719200"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/12483"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M705674200"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0161-5890(99)00141-8"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1742-4658.2010.07785.x"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1389-1723(04)70183-8"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1042\/BJ20051739"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/0263-7855(94)80102-9"},{"key":"e_1_2_7_14_1","first-page":"535","article-title":"A rapid reproducible test for determining rabies neutralizing antibody","volume":"48","author":"Smith J.","year":"1973","journal-title":"Bull. 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