Morgan E L, Hugli T E, Weigle W O
Proc Natl Acad Sci U S A. 1982 Sep;79(17):5388-91. doi: 10.1073/pnas.79.17.5388.
A 24-amino acid residue peptide has been isolated from the Fc region of a human IgG1 myeloma protein. The peptide has associated with it the same ability to induce murine B cells to polyclonally secrete antibody as does the intact Fc fragment. Amino acid composition of the peptide indicates that on a mole/mole basis the isolated peptide is identical to that published for residues 335-358 in the Eu IgG1 sequence. This peptide corresponds roughly to the first 24 amino acids of the CH3 domain. It is believed that the immunoregulatory properties that have been ascribed to the Fc fragment are associated with this peptide.
一种由24个氨基酸残基组成的肽已从人IgG1骨髓瘤蛋白的Fc区域分离出来。该肽与完整的Fc片段一样,具有诱导鼠B细胞多克隆分泌抗体的能力。该肽的氨基酸组成表明,在摩尔/摩尔基础上,分离出的肽与已发表的Eu IgG1序列中335 - 358位残基相同。此肽大致对应于CH3结构域的前24个氨基酸。据信,归因于Fc片段的免疫调节特性与该肽有关。