免疫グロブリンの構造

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書誌事項

タイトル別名
  • Structure of Immunoglobulin
  • メンエキ グロブリン ノ コウゾウ

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抄録

X-ray crystallographic studies show that the four domains of the H chain and two domains of the L chain in immunoglobulin G have very similar tertiary structures referred to as immunoglobulin fold and consist of two β-sheets. The states of tryptophyl, tyrosyl, hhistidyl residues, and disulfide bonds of Bence Jones proteins determined by physical and chemical methods are described. The VL domain is more resistant against denaturants than the CL domain. Studies on refolding of Bence Jones proteins from 4 M GuHCl shows that the VL domain refolds much faster than the CL domain. The noncovalent interaction of L chain to one of the two sites on H chain dimer decreases the affinity of the other site for L chain. The mechanism of formation of interchain disulfide bonds in Bence Jones proteins, Fab fragments, and immunoglobulin G is described.

収録刊行物

  • 生物物理

    生物物理 19 (2), 93-99, 1979

    一般社団法人 日本生物物理学会

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