{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T18:56:35Z","timestamp":1789757795954,"version":"4.0.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1994,5,15]]},"abstract":"<jats:p>In brain and many other tissues, type I inositol 1,4,5-trisphosphate (InsP3) 5-phosphatase is the major isoenzyme hydrolysing the calcium-mobilizing second messenger InsP3. This protein has been purified to apparent homogeneity from a crude soluble fraction of bovine brain, yielding a single major protein band with a molecular mass of 43 kDa after SDS\/PAGE. This material was used to determine internal microsequences. A partial DNA sequence has been amplified by PCR by using degenerate primers deduced from two protein sequences (FKAKKYKKV and DENYKSQE). A cDNA clone (BVCT) was isolated by screening a dog thyroid cDNA library. The encoded protein of 412 amino acids has a calculated molecular mass of 47,681 Da. Peptide sequences generated from the bovine brain enzyme were found to be 96% conserved compared with the dog thyroid protein. When clone BVCT was expressed in Escherichia coli, the recombinant protein was shown to hydrolyse both InsP3 and inositol 1,3,4,5-tetrakisphosphate, with apparent Km values of 28 and 3 microM respectively. Enzyme activity was inhibited by EDTA and 2,3-bisphosphoglycerate, both inhibitors of native InsP3 5-phosphatase, but not by EGTA and LiCl, as previously shown for the bovine brain enzyme. Our data show the cloning of type I InsP3 5-phosphatase which, interestingly, does not share any significant sequence identity with the previously cloned type III isoenzyme.<\/jats:p>","DOI":"10.1042\/bj3000085","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:37:53Z","timestamp":1439242673000},"page":"85-90","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":37,"title":["Cloning and expression in <i>Escherichia coli<\/i> of a dog thyroid cDNA encoding a novel inositol 1,4,5-trisphosphate 5-phosphatase"],"prefix":"10.1042","volume":"300","author":[{"given":"B","family":"Verjans","sequence":"first","affiliation":[{"name":"Interdisciplinary Research Institute (IRIBHN), Campus Erasme, Bldg. C, 808 route de Lennik, 1070 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F","family":"De Smedt","sequence":"additional","affiliation":[{"name":"Interdisciplinary Research Institute (IRIBHN), Campus Erasme, Bldg. C, 808 route de Lennik, 1070 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R","family":"Lecocq","sequence":"additional","affiliation":[{"name":"Interdisciplinary Research Institute (IRIBHN), Campus Erasme, Bldg. C, 808 route de Lennik, 1070 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V","family":"Vanweyenberg","sequence":"additional","affiliation":[{"name":"Interdisciplinary Research Institute (IRIBHN), Campus Erasme, Bldg. C, 808 route de Lennik, 1070 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C","family":"Moreau","sequence":"additional","affiliation":[{"name":"Interdisciplinary Research Institute (IRIBHN), Campus Erasme, Bldg. C, 808 route de Lennik, 1070 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C","family":"Erneux","sequence":"additional","affiliation":[{"name":"Interdisciplinary Research Institute (IRIBHN), Campus Erasme, Bldg. C, 808 route de Lennik, 1070 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/300\/1\/85\/613467\/bj3000085.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/300\/1\/85\/613467\/bj3000085.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T22:50:00Z","timestamp":1637707800000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/300\/1\/85\/30780\/Cloning-and-expression-in-Escherichia-coli-of-a"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1994,5,15]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1994,5,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3000085","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1994,5,15]]}}}