作者: F S Sharief , S S Li
DOI: 10.1016/S0021-9258(18)33344-1
关键词:
摘要: The low molecular weight, glutamine-rich storage protein isolated from the seeds of Ricinus communis (castor beans) has been shown to consist two different polypeptide chains linked by disulfide bond(s). small subunit is composed 34 amino acids with a proline at its NH2 terminus, whereas large contains 61 cyclized glutamine as NH2-terminal residue. complete acid sequence both subunits determined through characterization and selected peptides trypsin, chymotrypsin, thermolysin, cyanogen bromide cleavage. intact possesses number glutaminyl half-cystinyl residues exhibits heterogeneity observed peptide sequences. Comparison this those other seed proteins indicates some structural similarities between them. sequences castor bean are: (formula, see text).