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Characterization of Alpha-amylase Inhibitor in Vigna sublobata

Vigna sublobata之α-amylase(α-澱粉水解酶)抑制劑之性狀

摘要


本文描述來自Vigna sublobata之α-澱粉水解酶的抑制蛋白的性狀,該蛋白可抑制昆蟲(Callosobruchus analis)腸道之α-水解酶。SDS-電泳分析顯示該純化之抑制蛋白分子量為14,000。該抑制蛋白係非醣化者;而N-端序列(A P S P V...)類似來自Phaseolus vulgaris之α-AI-1,它的PI值為6.0。它主要位於子葉。當種子發芽後第一天到第五天該抑制蛋白之活性逐漸下降。而當種子發育形成階段(即授粉後直到第三十天)該抑制蛋白含量逐漸增加。

關鍵字

α-澱粉水解酶

並列摘要


Abstract. 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 14kDa 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.

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