Bharali Sangeeta, Chrungoo Nikhil K
Department of Botany, North Eastern Hill University Shillong 793 022, India.
Phytochemistry. 2003 May;63(1):1-5. doi: 10.1016/s0031-9422(02)00755-0.
The paper describes the amino acid sequence of a 26 kDa basic subunit of 13S globulin of common buckwheat (Fagopyrum esculentum Moench). The protein has 93 and 75% sequence homology with 11S globulin of Coffea arabica and beta subunit of 11S globulin of Cucurbita pepo respectively. The subunit has the "globally conserved" N-terminal sequence consisting of Gly-Ile-Asp-Glu and the cysteine at P7' from the proteolytic processing site. A conserved 7 residue domain of Pro-His-Trp-Asn-Ile-Asn-Ala, characteristic of basic subunits of legumins from non-leguminous angiosperms, is also present in this protein. A distinguishing features of this subunit is the relatively high level of lysine and methionine.
该论文描述了普通荞麦(苦荞麦)13S球蛋白26 kDa碱性亚基的氨基酸序列。该蛋白质与阿拉伯咖啡11S球蛋白以及西葫芦11S球蛋白β亚基的序列同源性分别为93%和75%。该亚基具有由甘氨酸-异亮氨酸-天冬氨酸-谷氨酸组成的“全局保守”N端序列,以及来自蛋白水解加工位点P7'处的半胱氨酸。一个由脯氨酸-组氨酸-色氨酸-天冬酰胺-异亮氨酸-天冬酰胺-丙氨酸组成的保守7残基结构域,这是来自非豆科被子植物豆球蛋白碱性亚基的特征,在该蛋白质中也存在。该亚基的一个显著特征是赖氨酸和蛋氨酸的含量相对较高。