Smith D J, Shulman S
Clin Exp Immunol. 1978 Mar;31(3):341-50.
A subunit of succinylated (40:1 molar ratio, succinic anhydride:lysine residues) human thyroglobulin (Tg) was prepared by gel filtration on 6% and 4% agarose. This subunit (S-8) had a sdegrees20, w of 7.6S, Ddegrees20, w of 2.96 x 10(7) and an equilibrium molecular weight of 165,000 after correction for bound succinic anhydride (SA). The S-8 component was suggested to be a quarter unit of intact Tg. The S-8 and intact Tg had nearly identical amino acid compositions with differences only in glutamic acid, glycine and proline. The iodine content of both components was similar. The succinylated S-8 subunit, as well as material which sedimented with a value of 2S or less, retained some but not all heteroantigenic and autoantigenic sites in immunodiffusion and inhibition of passive hemagglutination.
通过在6%和4%琼脂糖上进行凝胶过滤制备了琥珀酰化（琥珀酸酐与赖氨酸残基的摩尔比为40:1）人甲状腺球蛋白（Tg）的一个亚基。该亚基（S-8）的沉降系数s₂₀,w为7.6S，扩散系数D₂₀,w为2.96×10⁻⁷，校正结合的琥珀酸酐（SA）后平衡分子量为165,000。S-8组分被认为是完整Tg的四分之一单位。S-8和完整Tg的氨基酸组成几乎相同，仅在谷氨酸、甘氨酸和脯氨酸方面存在差异。两种组分的碘含量相似。琥珀酰化的S-8亚基以及沉降值为2S或更小的物质在免疫扩散和被动血凝抑制中保留了一些但并非全部的异源抗原和自身抗原位点。
