The biosynthesis and primary structure of pea seed lectin.

摘要: Isolation of pea lectin from immature seeds, together with in vivo pulse-chase labeling and vitro translation RNA such all gave results which indicated strongly that is initially synthesized as a large precursor (pre-pro-form) (Mr = 25,000) cleaved both co- post-translationally to yield the alpha beta subunits mature lectin. Two overlapping cDNA plasmids complementary mRNA were sequenced. They coded for lectin, orientation leads NH2 terminus, hydrophobic NH2-terminal leader sequence included 3' untranslated region 124 nucleotides. In appropriate reading frame, no stop codon was found between coding sequences subunits, confirming synthesis via pre-pro-form. The entire showed high degree homology published amino acid lectins lentil, broad bean, and, lesser extent, concanavalin A jack bean. Sequence variation occurred mainly those regions thought not be involved metal- sugar-binding or formation beta-pleated sheets.