{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T02:16:33Z","timestamp":1773627393335,"version":"3.50.1"},"reference-count":29,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2005,1,15]],"date-time":"2005-01-15T00:00:00Z","timestamp":1105747200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2005,1,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            In this study, the dipeptidyl peptidase IV (DPP IV) of the swine pathogen\n            <jats:italic>Streptococcus suis<\/jats:italic>\n            was cloned, overexpressed in\n            <jats:italic>Escherichia coli<\/jats:italic>\n            , and characterized. The coding region comprises 2,268 nucleotides containing an open reading frame that codes for a 755-amino-acid protein with a calculated molecular mass of 85 kDa. The amino acid sequence contained the sequence Gly-X-Ser-X-X-Gly, which is a consensus motif flanking the active-site serine shared by serine proteases. The recombinant DPP IV showed a high affinity for the synthetic peptide glycine-proline-\n            <jats:italic>p<\/jats:italic>\n            -nitroanilide and was strongly inhibited by Hg\n            <jats:sup>2+<\/jats:sup>\n            and diprotin A.\n          <\/jats:p>","DOI":"10.1128\/jb.187.2.795-799.2005","type":"journal-article","created":{"date-parts":[[2005,1,3]],"date-time":"2005-01-03T18:33:17Z","timestamp":1104777197000},"page":"795-799","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":18,"title":["Cloning, Purification, and Enzymatic Properties of Dipeptidyl Peptidase IV from the Swine Pathogen\n            <i>Streptococcus suis<\/i>"],"prefix":"10.1128","volume":"187","author":[{"given":"Marie-Claude","family":"Jobin","sequence":"first","affiliation":[{"name":"Groupe de Recherche en E\u0301cologie Buccale, Faculte\u0301 de Me\u0301decine Dentaire, Universite\u0301 Laval, Quebec City"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gabriela","family":"Martinez","sequence":"additional","affiliation":[{"name":"Groupe de Recherche sur les Maladies Infectieuses du Porc, Faculte\u0301 de Me\u0301decine Ve\u0301te\u0301rinaire, Universite\u0301 de Montre\u0301al"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Julie","family":"Motard","sequence":"additional","affiliation":[{"name":"Groupe de Recherche en E\u0301cologie Buccale, Faculte\u0301 de Me\u0301decine Dentaire, Universite\u0301 Laval, Quebec City"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marcelo","family":"Gottschalk","sequence":"additional","affiliation":[{"name":"Groupe de Recherche sur les Maladies Infectieuses du Porc, Faculte\u0301 de Me\u0301decine Ve\u0301te\u0301rinaire, Universite\u0301 de Montre\u0301al"},{"name":"Canadian Research Network on Bacterial Pathogens of Swine, Natural Sciences and Engineering Research Council of Canada, Saint-Hyacinthe, Quebec, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel","family":"Grenier","sequence":"additional","affiliation":[{"name":"Groupe de Recherche en E\u0301cologie Buccale, Faculte\u0301 de Me\u0301decine Dentaire, Universite\u0301 Laval, Quebec City"},{"name":"Canadian Research Network on Bacterial Pathogens of Swine, Natural Sciences and Engineering Research Council of Canada, Saint-Hyacinthe, Quebec, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1177\/00220345850640020201","volume":"64","year":"1985","unstructured":"Abiko, Y., M. 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