{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,4]],"date-time":"2025-11-04T15:58:43Z","timestamp":1762271923030},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1991,11,15]]},"abstract":"<jats:p>T-kininogen, the major kininogen in rat plasma, releases Ile-Ser-bradykinin (T-kinin) when incubated with trypsin, but is not a substrate for tissue kallikrein. Enzymes able to release T-kinins from T-kininogen have been found in the rat submandibular gland, but precise identification of these enzymes and their possible relationship to kallikrein-like enzymes has not been established. We studied T-kininogenase activity in fractionated submandibular gland homogenate. The main T-kininogen catalytic enzyme was purified and characterized, and found to be identical to antigen gamma, a kallikrein-like enzyme which we have previously characterized. Of other identified kallikrein-like enzymes only tonin showed weak T-kininogenase activity, which was about 0.25% of that of antigen gamma. No other T-kininogen catalytic enzymes were observed. Antigen gamma released a kinin which was identified as T-kinin by reverse-phase h.p.l.c. The T-kininogenase activity of antigen gamma had a Km of 29 +\/- 4 microM and a kcat\/Km of 140 M-1.s-1, and was comparable with its high and low molecular mass-kininogenase activity (7.4 and 10 micrograms of kinin\/h per mg respectively). In contrast, tissue kallikrein released 0.2 and 42,200 micrograms of kinin\/h per mg respectively. Thus antigen gamma is a weak kininogenase. The isoelectric point of antigen gamma, but not its molecular mass, differed from that of other kallikrein-like enzymes. Isoelectrofocusing in flat-bed gels combined with immunostaining was therefore a convenient method for identification. The kallikrein-like nature of antigen gamma was demonstrated by its immunological similarity to tissue kallikrein and tonin and by 91% and 87% amino acid sequence similarity with tonin and kallikrein respectively (67 amino acids sequenced). Complete identity was also not observed with other sequenced kallikrein genes, mRNAs or proteins.<\/jats:p>","DOI":"10.1042\/bj2800019","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:24:15Z","timestamp":1439241855000},"page":"19-25","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["T-kininogenase activity of the rat submandibular gland is predominantly due to the kallikrein-like serine protease antigen <i>\u03b3<\/i>"],"prefix":"10.1042","volume":"280","author":[{"given":"T","family":"Berg","sequence":"first","affiliation":[{"name":"Institute of Physiology, Medical Faculty, University of Oslo, Oslo, Norway"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"I","family":"Wassdal","sequence":"additional","affiliation":[{"name":"Institute of Physiology, Medical Faculty, University of Oslo, Oslo, Norway"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"T","family":"Mindroiu","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Faculty of Science, University of Oslo, Oslo, Norway"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K","family":"Sletten","sequence":"additional","affiliation":[{"name":"Hypertension Research Division, Henry Ford Hospital, Detroit, MI, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G","family":"Scicli","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Faculty of Science, University of Oslo, Oslo, Norway"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"O A","family":"Carretero","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Faculty of Science, University of Oslo, Oslo, Norway"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A G","family":"Scicli","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Faculty of Science, University of Oslo, Oslo, Norway"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/280\/1\/19\/605079\/bj2800019.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/280\/1\/19\/605079\/bj2800019.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T15:27:49Z","timestamp":1637681269000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/280\/1\/19\/27222\/T-kininogenase-activity-of-the-rat-submandibular"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1991,11,15]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1991,11,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2800019","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1991,11,15]]}}}