Please use this identifier to cite or link to this item:
|Type:||Artigo de periódico|
|Title:||Cloning And Characterization Of A Cdna Encoding A Sulfur-rich Coixin|
|Abstract:||A full-length cDNA clone encoding a sulfur-rich Coix prolamin was isolated using a cDNA library constructed from polysomal mRNA prepared from immature Coix endosperm. The deduced amino acid sequence of the cDNA clone predicted a polypeptide of 194 residues, which shared 64% homology with the 17 kDa β-zein. The mature protein contains the familiar composition of the prolamins and an unusually high content of the sulfur-containing amino acids methionine (11.6%) and cysteine (5.2%). In vitro transcription followed by in vitro translation of the coding region of the pBCX17.9S clone gave rise to a polypeptide with an apparent molecular weight corresponding to the C4 α-coixin. Hydropathy analysis showed that C4 α-coixin is slightly more hydrophobic than β-zein. © 1992 Kluwer Academic Publishers.|
|Editor:||Kluwer Academic Publishers|
|Citation:||Plant Molecular Biology. Kluwer Academic Publishers, v. 18, n. 1, p. 171 - 174, 1992.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.