{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,7]],"date-time":"2026-02-07T21:44:55Z","timestamp":1770500695478,"version":"3.49.0"},"reference-count":21,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2008,6,28]],"date-time":"2008-06-28T00:00:00Z","timestamp":1214611200000},"content-version":"vor","delay-in-days":5080,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[1994,8]]},"abstract":"<jats:p>The soybean seed basic 7S globulin (Bg) is capable of binding bovine insulin and insulin\u2010like growth factors, and has protein kinase activity which corresponds to about two thirds of the tyrosine kinase activity of the rat insulin receptor. A 4\u2010kDa peptide named leginsulin, which can bind to Bg and compete with insulin for binding to Bg, was isolated from radicles of germinated soybean seeds. The leginsulin had a stimulatory effect on the phosphorylation activity of Bg, suggesting that it is involved in cellular signal transduction. The leginsulin was sequenced by automated Edman degradation and electrospray ionization mass spectrometry. It consisted of 37 amino acid residues with six half\u2010cystines in three disulfide bridges. The mass spectrometric analysis revealed that a portion of the peptide is processed to delete the C\u2010terminal glycine like a number of animal peptide hormones, but not C\u2010terminally amidated. The cDNA encoding the leginsulin was cloned, sequenced and considered to code for a precursor polypeptide consisting of a putative signal peptide, the leginsulin, a linker peptide, a 6\u2010kDa peptide and a C\u2010terminal peptide. Although there is no sequence similarity between the leginsulin and insulin or insulin\u2010like growth factors, the leginsulin is a possible candidate for plant peptide hormones.<\/jats:p>","DOI":"10.1111\/j.1432-1033.1994.tb20008.x","type":"journal-article","created":{"date-parts":[[2005,3,4]],"date-time":"2005-03-04T07:41:29Z","timestamp":1109922089000},"page":"167-172","source":"Crossref","is-referenced-by-count":64,"title":["A Peptide that Stimulates Phosphorylation of the Plant Insulin\u2010Binding Protein"],"prefix":"10.1111","volume":"224","author":[{"given":"Yoshihiro","family":"Watanabe","sequence":"first","affiliation":[]},{"given":"Sergei F.","family":"Barbashov","sequence":"additional","affiliation":[]},{"given":"Setsuko","family":"Komatsu","sequence":"additional","affiliation":[]},{"given":"Andrew M.","family":"Hemmings","sequence":"additional","affiliation":[]},{"given":"Masaru","family":"Miyagi","sequence":"additional","affiliation":[]},{"given":"Susumu","family":"Tsunasawa","sequence":"additional","affiliation":[]},{"given":"Hisashi","family":"Hirano","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2008,6,28]]},"reference":[{"key":"e_1_2_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-291X(88)81049-0"},{"key":"e_1_2_2_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00217a014"},{"key":"e_1_2_2_4_2","first-page":"421","article-title":"Isolation and characterization of soybean insulin\u2010binding proteins","volume":"17","author":"Barbashov S. 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