Cameron P M, Limjuco G A, Chin J, Silberstein L, Schmidt J A
J Exp Med. 1986 Jul 1;164(1):237-50. doi: 10.1084/jem.164.1.237.
Two anionic species of human IL-1 have been purified to homogeneity. These molecules were characterized as having pI of 5.4 and 5.2 and molecular weights identical to IL-1/6.8 (17,500). The specific activities of IL-1/5.4 and IL-1/5.2, as measured in the mouse thymocyte co-mitogenic assay, were identical to that of IL-1/6.8, namely 1.2 X 10(7) U/mg, with half-maximal stimulation observed at 2 X 10(-11) M. IL-1/5.4 and IL-1/5.2 were found to be antigenically distinct from IL-1/6.8 in an ELISA. IL-1/5.4 was structurally distinct from IL-1/6.8 based on reverse-phase HPLC or CNBr peptides. Intact IL-1/5.2 and three intact CNBr peptides of IL-1/5.4 were sequenced, with the identification of 74 amino acid residues. These sequences were found to correspond exactly with the amino acid sequence deduced from the IL-1-alpha cDNA reported by March et al.
已将人白细胞介素-1的两种阴离子形式纯化至同质。这些分子的特征为其等电点分别为5.4和5.2,分子量与白细胞介素-1/6.8(17,500)相同。在小鼠胸腺细胞共促有丝分裂试验中测得的白细胞介素-1/5.4和白细胞介素-1/5.2的比活性与白细胞介素-1/6.8相同,即1.2×10⁷U/mg,在2×10⁻¹¹M时观察到半数最大刺激。在酶联免疫吸附测定中发现白细胞介素-1/5.4和白细胞介素-1/5.2在抗原性上与白细胞介素-1/6.8不同。基于反相高效液相色谱法或溴化氰肽,白细胞介素-1/5.4在结构上与白细胞介素-1/6.8不同。测定了完整的白细胞介素-1/5.2和白细胞介素-1/5.4的三个完整溴化氰肽的序列,鉴定出74个氨基酸残基。发现这些序列与March等人报道的白细胞介素-1-α cDNA推导的氨基酸序列完全一致。