AMINO ACID SEQ OF NEW ALLERGENIC ALBUMIN STORAGE PROTEIN FROM RICINUS COMMUNIS

一种新的2S白蛋白的分离和序列测定 描述了来自蓖麻种子的贮藏蛋白。 的 使用选择性酶切的片段方法 降解和质谱法用于证明主要 11.3 kDa异二聚体蛋白的结构，其通过4 二硫桥 采用质谱（MALDI-TOF和ESI/MS） 以获得蛋白质及其两种组分的分子量， 链作为验证每条链的序列的标准 通过湿化学获得。 氨基端封闭的序列 通过ESI/MS测定肽<Gln Gln Gln Glu， 用湿化学来做。 第二个2S的特征 白蛋白，从R communis种子表明，237残基， 前体蛋白基于cDNA数据编码两个 不同的异源二聚体蛋白质含有约97个残基。 描述这项工作的手稿已出版J.G odinho da 小席尔瓦，O.L. T马查多角泉，J.C. Padovan，B.T. Chait，U.A. Mirza & L. J.格林“一种新的变应原2S的氨基酸序列 来自蓖麻的白蛋白储存蛋白，其是30 kDa前体蛋白”Archives of Biochem. & Biophys. 第336（1996）号决议 10-18.

The isolation and sequence determination of a new 2S albumin storage protein from Ricinus communis seeds is described. The fragment approach using selective enzymatic cleavage, Edman degradation and mass spectrometry was used to demonstrate primary structure of the 11.3 kDa heterodimer protein which is linked by 4 disulfide bridges. Mass spectrometry (MALDI-TOF and ESI/MS) were used to obtain the molecular weight of the protein and its two constituent chains as a criterion for validating the sequence of each chain obtained by wet chemistry. The sequence of the amino terminal blocked peptide <Gln Gln Gln Glu was determined by ESI/MS which was impossible to do by wet chemistry. The characterization of the second 2S albumin, from R communis seeds demonstrates that the 237 residue precursor protein postulated on the basis on cDNA data codes for two different heterodimer proteins containing approximately 97 residues. A manuscript describing this work has been published J.G odinho da Silva, Jr., O.L.T. Machado, C. Izumi, J.C. Padovan, B.T. Chait, U.A. Mirza & L.J. Greene "Amino acid sequence of a new allergenic 2S albumin storage protein from Ricinus communis which is part of a 30 kDa precursor protein" Archives of Biochem. & Biophys. 336 (1996) 10-18.