Purification and characterization of moschins, arginine-glutamate-rich proteins with translation-inhibiting activity from brown pumpkin (Cucurbita moschata) seeds.
From fresh brown pumpkin seeds, two proteins with a molecular mass of 12kDa and an N-terminal sequence rich in arginine and glutamate residues were obtained. The protein designated alpha-moschin closely resembled the fruitfly programmed-cell death gene product and the protein designated beta-moschin demonstrated striking similarity to prepro 2S albumin in N-terminal sequence. alpha- and beta-moschins inhibited translation in the rabbit reticulocyte lysate system with an IC(50) of 17 microM and 300nM, respectively.
D000595:Amino Acid Sequence; D001120:Arginine / Q000032:analysis*; D028464:Cucurbita / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D005971:Glutamates / Q000032:analysis*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification* / Q000494:pharmacology; D014176:Protein Biosynthesis / Q000187:drug effects*; D012639:Seeds / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D005971:Glutamates; D010940:Plant Proteins; D001120:Arginine