半胱氨酸
丝氨酸
化学
残留物(化学)
丙氨酸
免疫球蛋白轻链
氨基酸
碘乙酸
立体化学
生物化学
抗体
酶
生物
免疫学
作者
Hongcheng Liu,Suju Zhong,Chris Chumsae,Czeslaw Radziejewski,Chung-Ming Hsieh
标识
DOI:10.1016/j.ab.2010.09.025
摘要
The light chain cysteine residue that forms an interchain disulfide bond with the cysteine residue in the heavy chain in IgG1κ is the last amino acid. The cysteine residue is followed by a serine residue in IgG1λ. Effect of the serine residue on the susceptibility of disulfide bonds to reduction was investigated in the current study using a method including reduction, differential alkylation using iodoacetic acid with either natural isotopes or enriched with carbon-13, and mass spectrometry analysis. This newly developed method allowed an accurate determination of the susceptibility of disulfide bonds in IgG antibodies. The effect of the serine residue on disulfide bond susceptibility was compared using three antibodies with differences only in the light chain last amino acid, which was either a serine residue, an alanine residue or deleted. The results demonstrated that the presence of the amino acid (serine or alanine) increased the susceptibility of the inter light and heavy chain disulfide bonds to reduction. On the other hand, susceptibility of the two inter heavy chain disulfide bonds and intrachain disulfide bonds was not changed significantly.
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