Staswick P E, Hermodson M A, Nielsen N C
J Biol Chem. 1981 Aug 25;256(16):8752-5.
Five complexes consisting of one acidic and one basic subunit that were linked via disulfide bonds were purified from unreduced S-alkylated glycinin. The acidic and basic subunits were identified unambiguously using NH2-terminal sequence analysis, sodium dodecyl sulfate (SDS)-electrophoresis, and analytical isoelectric focusing. The subunit pairings are A1aB2, A1bB1b, A2B1a, A3B4, and F2(2)B3. Polypeptide A4 was not linked to a corresponding basic subunit via a disulfide bond. The study shows that pairing between subunits is nonrandom, which is consistent with evidence that glycinin is synthesized as a Mr = 60,000 precursor that undergoes post-translational modification to form the individual linked subunits.
从不还原的S-烷基化大豆球蛋白中纯化出由一个酸性亚基和一个碱性亚基通过二硫键相连组成的五个复合物。使用氨基末端序列分析、十二烷基硫酸钠(SDS)电泳和分析等聚焦法明确鉴定了酸性和碱性亚基。亚基配对为A1aB2、A1bB1b、A2B1a、A3B4和F2(2)B3。多肽A4未通过二硫键与相应的碱性亚基相连。该研究表明亚基之间的配对是非随机的,这与大豆球蛋白作为Mr = 60,000前体合成并经过翻译后修饰形成各个相连亚基的证据一致。