{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T18:33:58Z","timestamp":1791311638186,"version":"4.3.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1995,1,1]]},"abstract":"<jats:p>A soluble protein kinase purified from winged bean (Psophocarpus tetragonolobus) shoots, has been assessed as a monomeric enzyme with an approximate M(r) of 60,000 in spite of the presence of two polypeptides of 61 and 58 kDa determined by SDS\/PAGE. Immunoblot analyses using either of the two antisera raised individually against the polypeptides, detect both of them in purified preparations and a single larger polypeptide (62 kDa) in freshly prepared tissue homogenates, clearly indicating the likelihood of the doublet being formed from the larger one by proteolysis. Histone H1, syntide 2 and a synthetic myosin light chain-related peptide (MLC-peptide) have been identified as exogenous substrates of the enzyme. Complete Ca(2+)-dependence for substrate phosphorylation, a drastic inhibition of the reaction by a calmodulin (CaM) antagonist which can be partially reversed by a heterologous CaM and direct 45Ca(2+)-binding on blot, form compelling evidence in favour of a CaM-like domain of the enzyme. Both the polypeptides of the purified enzyme undergo intramolecular autophosphorylation on serine residue(s). Unlike the substrate phosphorylation reaction, autophosphorylation is Ca(2+)-independent and is not inhibited by the CaM antagonist. Down-regulation of substrate phosphorylation by auto-phosphorylation, and stimulation of the autophosphorylation by histone H1 and MLC-peptide, are novel regulatory features of the enzyme.<\/jats:p>","DOI":"10.1042\/bj3050205","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:41:21Z","timestamp":1439242881000},"page":"205-210","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":37,"title":["Characterization of a winged bean (<i>Psophocarpus tetragonolobus<\/i>) protein kinase with calmodulin-like domain: regulation by autophosphorylation"],"prefix":"10.1042","volume":"305","author":[{"given":"P","family":"Saha","sequence":"first","affiliation":[{"name":"Indian Institute of Chemical Biology, 4 Raja SC Mullick Road, Calcutta 700032, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M","family":"Singh","sequence":"additional","affiliation":[{"name":"Indian Institute of Chemical Biology, 4 Raja SC Mullick Road, Calcutta 700032, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/305\/1\/205\/614720\/bj3050205.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/305\/1\/205\/614720\/bj3050205.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T23:20:31Z","timestamp":1637709631000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/305\/1\/205\/31575\/Characterization-of-a-winged-bean-Psophocarpus"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,1,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1995,1,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3050205","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1995,1,1]]}}}