构成抗原特异性抑制因子分泌形式的两种基因产物之间存在链间二硫键。
Presence of interchain disulfide bonds between two gene products that compose the secreted form of an antigen-specific suppressor factor.
作者信息
Taniguchi M, Saito T, Takei I, Tokuhisa T
出版信息
J Exp Med. 1981 Jun 1;153(6):1672-7. doi: 10.1084/jem.153.6.1672.
Abstract
The secreted form of the suppressor T cell factor specific for keyhole limpet hemocyanin derived from the hybridoma 34S-704 was found to consist of the two distinct polypeptide chains, i.e., the antigen-binding and the I-J-encoded chains. They were linked in covalent association with disulfide bonds. The two chains were cleaved by the reduction with dithiothreitol and were easy to reconstitute the active form of TsF. The association of the two distinct chains was suggested to be essential for the expression of the TsF activity.
摘要
发现源自杂交瘤34S - 704的对钥孔戚血蓝蛋白特异的抑制性T细胞因子的分泌形式由两条不同的多肽链组成，即抗原结合链和I-J编码链。它们通过二硫键共价相连。用二硫苏糖醇还原可使两条链裂解，并且很容易重新构建TsF的活性形式。两条不同链的缔合被认为对TsF活性的表达至关重要。
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