{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2022,11,25]],"date-time":"2022-11-25T18:51:11Z","timestamp":1669402271581},"reference-count":7,"publisher":"Walter de Gruyter GmbH","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1999,1,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The large and varied multigene families of tissue kallikreins of rat and mouse are considered to selectively release as many bioactive peptides. In order to determine whether a similar family of enzymes is expressed in the organs of the guinea pig purification studies were performed. Tissue kallikreins from the submandibular gland, coagulating gland\/prostate complex and the pancreas were separated by affinity chromatography on benzamidine-Sepharose. Amino-terminal sequences, the patterns of hydrolysis rates of a number of peptide<\/jats:p><jats:p>Guinea pig tissue kallikreins 1 and 2 have been reported previously. In the present study we have identified a third type, designated tissue kallikrein 1a because of its sequence similarity to kallikrein 1, which differs from the latter in the catalytic properties. The inferred occurrence of not more than two or three independent tissue kallikrein genes in the guinea pig contrasts with the varied family of enzymes expressed by the large number of such genes present in rats and mice. Expression in the guinea pig (and also in humans) of only a small number of tissue kallikreins makes specific processing of a multitude of biologically active peptides by such enzymes unlikely.<\/jats:p>","DOI":"10.1515\/bc.1999.008","type":"journal-article","created":{"date-parts":[[2004,9,29]],"date-time":"2004-09-29T11:59:40Z","timestamp":1096459180000},"source":"Crossref","is-referenced-by-count":11,"title":["Not More than Three Tissue Kallikreins Identified from Organs of the Guinea Pig"],"prefix":"10.1515","volume":"380","author":[{"given":"F.","family":"Fiedler","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G.","family":"Betz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H.","family":"Hinz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"F.","family":"Lottspeich","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D.M.","family":"Raidoo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K.D.","family":"Bhoola","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"374","reference":[{"key":"ref701","first-page":"628","article-title":"Further purification and properties of kininogenase from the guinea pig s coagulating gland","volume":"22","author":"Oliveira","year":"1987","journal-title":"Chem Pharm Bull"},{"key":"ref691","first-page":"303","article-title":"Nature Tissue kallikreins of the guinea - pig","author":"Mayer","year":"1989","journal-title":"Med Biol"},{"key":"ref671","first-page":"3928","article-title":"Acad Dra","volume":"80","author":"Markwardt","journal-title":"Sci USA"},{"key":"ref721","first-page":"121","article-title":"pp Characterisation of the human kallikrein locus Primary structure of a human glandular kallikrein gene DNA Substrate binding site in bovine chymotrypsin A - gamma A crystallographic study using peptide chloromethyl ketones as site - specific inhibitors","volume":"14","author":"Riegman","year":"1992","journal-title":"Genomics Biochemistry"},{"key":"ref681","first-page":"401","article-title":"wert Amino - alkyl - benzol - sulfo - fluoride als Fermentinhibitoren Structure of mouse kallikrein gene family suggests a role in specific processing of biologically active peptides","volume":"26","author":"Landmann","year":"1971","journal-title":"Pharmazie"},{"key":"ref711","first-page":"5032","article-title":"Substrate activation of porcine pancreatic kallikrein by N derivatives of arginine - nitroanilides In : Chemistry and Biolo - gy of the Kallikrein - Kinin System in Health and Disease and Austen eds ( USA : Government Printing Office )","volume":"26","author":"Pierce","year":"1976","journal-title":"Biochemistry"},{"key":"ref631","first-page":"479","article-title":"Clin Isolation and characterisation of human urinary kallikrein Hoppe - Seyler s Z","volume":"15","author":"Geiger","year":"1980","journal-title":"Biochem"}],"container-title":["Biological Chemistry"],"original-title":[],"link":[{"URL":"http:\/\/www.degruyter.com\/view\/j\/bchm.1999.380.issue-1\/bc.1999.008\/bc.1999.008.xml","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/BC.1999.008\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,4,21]],"date-time":"2021-04-21T21:11:32Z","timestamp":1619039492000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/BC.1999.008\/html"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1999,1,4]]},"references-count":7,"journal-issue":{"issue":"1"},"URL":"https:\/\/doi.org\/10.1515\/bc.1999.008","relation":{},"ISSN":["1437-4315","1431-6730"],"issn-type":[{"value":"1437-4315","type":"electronic"},{"value":"1431-6730","type":"print"}],"subject":[],"published":{"date-parts":[[1999,1,4]]}}}