A peptide that stimulates phosphorylation of the plant insulin-binding protein. Isolation, primary structure and cDNA cloning.

摘要: The soybean seed basic 7S globulin (Bg) is capable of binding bovine insulin and insulin-like growth factors, has protein kinase activity which corresponds to about two thirds the tyrosine rat receptor. A 4-kDa peptide named leginsulin, can bind Bg compete with for Bg, was isolated from radicles germinated seeds. leginsulin had a stimulatory effect on phosphorylation suggesting that it involved in cellular signal transduction. sequenced by automated Edman degradation electrospray ionization mass spectrometry. It consisted 37 amino acid residues six half-cystines three disulfide bridges. spectrometric analysis revealed portion processed delete C-terminal glycine like number animal hormones, but not C-terminally amidated. cDNA encoding cloned, considered code precursor polypeptide consisting putative peptide, linker 6-kDa peptide. Although there no sequence similarity between or possible candidate plant hormones.