Characterization of Alpha-amylase inhibitor in Vigna sublobata
نویسندگان
چکیده
Alpha-amylase inhibitor protein, which inhibits the activity of insect (Callosobruchus analis) α-amylase, was characterized from V. sublobata. The molecular weight of purified inhibitor protein was 14 kDa by SDS-PAGE. The inhibitor is non-glycosylated protein and its N-terminal sequence is similar (A P S P V...) to Phaseolus vulgaris α-AI-1. Its pI value is 6.0 and largely localised in cotyledons. The inhibitory activity decreased during germination from days one to five. In the developmental stages of seed formation from anthesis to 30 days the inhibitor content increased.
منابع مشابه
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