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花生 2S 蛋白的提取分离及部分性质研究 被引量:22

SEPARATION,PURIFICATION AND CHARACTERIZATION OF 2S PROTEIN FROM PEANUT( ARACHIS HYPOGAEA L.)SEEDS
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摘要 用低盐缓冲液提取加热处理的方法分离了花生种子的2S蛋白组分,用激光质谱法测定了2S蛋白各组分的分子量;用高效液相色谱法测定了2S蛋白的氨基酸组成;用差示扫描量热法测定了2S蛋白的加工工艺性质.研究结果表明花生2S蛋白主要由17种多肽组成,富含Cys及Met等含硫氨基酸,且具有很强的耐热性与亲水性. An improved procedure was developed to extract,separate and purify the 2S protein from peanut ( Arachis hypogaea var.Yuoyu_116) seeds by low salt buffer and heat treatment followed by Sephadex G_100 gel filtration.The 2S protein fractions were resolved by 2D_PAGE into 17 polypeptides,whose molecular weight was determined by laser mass spectrometer.SDS_PAGE analysis and DSC thermogram indicated that 2S polypeptides were hydrophilic and heat stable whereas the arachin and conarachin were hydrophobic and heat labile.Some of the 2S proteins exhibited trypsin inhibitory activity.The result also showed that the soluble sugars facilitated vitrification of 2S proteins,by which prevented the crystallization of 2S protein during the withdrawn of water.
出处 《华南理工大学学报(自然科学版)》 EI CAS CSCD 北大核心 1998年第4期1-5,共5页 Journal of South China University of Technology(Natural Science Edition)
基金 国家自然科学基金 广东省博士启动基金
关键词 花生 2S蛋白 纯化 热稳定性 Arachis hypogaea 2S Protein purification heat stability
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参考文献3

  • 1Yun T,Biosci Biochem,1993年,57卷,940页
  • 2Wu C,J Agric Food Chem,1990年,38卷,1523页
  • 3杨晓泉,植物生理学报,1988年,24卷,2期,125页

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