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对人免疫球蛋白分子Kol的Fab片段和Fc片段进行的小角X射线研究。

Small-angle X-ray studies of the Fab and Fc fragments from the human immunoglobulin molecule Kol.

作者信息

Pilz I, Schwarz E, Palm W

出版信息

Eur J Biochem. 1976 Dec;71(1):239-47. doi: 10.1111/j.1432-1033.1976.tb11110.x.

Abstract

The conformation of the Fab and Fc fragments from the human immunoglobulin molecule Kol [IgI I, chi2gamma2, Gm(f)+] was studied by small-angle x-ray scattering in solution. The fragments were studied in 0.02 M Tris-HCl buffer. For the Fab fragment the radius of gyration was found to be 3.15 +/- 0.15 nm, the volume to be 75 +/- 8 nm3. For the Fc fragment the respective values were 3.15 +/- 0.15 nm for the radius of gyration and 91 +/- 8 nm3 for the volume. A large number of models were calculated for both fragments to find models which fit these data and have the same scattering curve. The models with the best agreement were compared with the models found for the crystalline state by crystal x-ray studies.

摘要

通过溶液中的小角X射线散射研究了来自人免疫球蛋白分子Kol [IgI I,chi2γ2,Gm(f)+]的Fab和Fc片段的构象。这些片段在0.02 M Tris-HCl缓冲液中进行研究。对于Fab片段,回转半径为3.15±0.15 nm,体积为75±8 nm3。对于Fc片段,回转半径和体积的相应值分别为3.15±0.15 nm和91±8 nm3。为这两个片段计算了大量模型,以找到符合这些数据并具有相同散射曲线的模型。将一致性最佳的模型与通过晶体X射线研究获得的晶体状态模型进行了比较。

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