Wingfield P, Pain R H, Craig S
FEBS Lett. 1987 Jan 26;211(2):179-84. doi: 10.1016/0014-5793(87)81432-1.
Recombinant produced human tumour necrosis factor (TNF) has been studied to characterise the subunit structure of the protein. TNF is shown to be a trimer Mr 52000 in which the subunits are associated in a compact, triangular form. In secondary structure it belongs to the all-beta class of proteins. It has high thermodynamic stability and the unfolded subunits can fold and associate spontaneously to form native, biologically active TNF.
已经对重组生产的人肿瘤坏死因子（TNF）进行了研究，以表征该蛋白质的亚基结构。TNF显示为三聚体，分子量为52000，其中亚基以紧密的三角形形式缔合。在二级结构中，它属于全β类蛋白质。它具有高的热稳定性，未折叠的亚基可以自发折叠并缔合形成天然的、具有生物活性的TNF。
