Ribosome inactivating protein and lectin from bitter melon (Momordica charantia) seeds: sequence comparison with related proteins.
One of the ribosome inactivating proteins (RIPs), beta-momorcharin, and a lectin were isolated from seeds of the bitter melon Momordica charantia (Family Cucurbitaceae) in accordance with published procedures. Both beta-momorcharin and M. charantia lectin were then subjected to amino acid sequencing. beta-momorcharin exhibited considerable homology in sequence to other Cucurbitaceae RIPs, and also to the A chains of abrin and ricin which are type II (double-chained) RIPs. The resemblance between alpha-momorcharin and other RIPs is closer than that between beta-momorcharins and other RIPs. M. charantia lectin manifested a certain extent of sequence similarity to beta-momorcharin and other RIPs, and some degree of homology in sequence to lectins from Cucurbita maxima, Cucurbita argyrosperma, Sambucus nigra and Ricinus Communis.
Wang
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Department of Microbiology, China Agricultural University, Beijing.
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D000595:Amino Acid Sequence; D019662:Cucurbitaceae / Q000737:chemistry*; D005638:Fruit / Q000737:chemistry; D037102:Lectins / Q000737:chemistry*; D008969:Molecular Sequence Data; D037121:Plant Lectins; D010940:Plant Proteins / Q000737:chemistry*; D011500:Protein Synthesis Inhibitors / Q000737:chemistry; D012269:Ribosomal Proteins; D054788:Ribosome Inactivating Proteins; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*; D012639:Seeds / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors; D012269:Ribosomal Proteins; C039582:MMC protein, Momordica charantia; D054788:Ribosome Inactivating Proteins