Abstract：
:The structure of a short-chain IgG2a antibody, which is a member of the family of mouse anti-dansyl switch variant antibodies with identical variable regions but different heavy-chain constant regions [Dangl, J.L., Parks, D. R., Oi, V. T., & Herzenberg, L. A. (1982) Cytometry 2, 395-401], is reported. Amino acid sequencing analyses have demonstrated that in the short-chain IgG2a antibody the entire CH1 domain is deleted whereas the hinge region remains intact. Small-angle X-ray scattering data were collected for the short-chain IgG2a antibody and compared with those for the switch variant IgG1, IgG2a, and IgG2b antibodies with the normal heavy chain. It has been concluded that deletion of the CH1 domain results in a large structural change and the short-chain IgG2a antibody possesses an elongated molecular shape with a much smaller hinge angle as compared with the normal IgG2a antibody that is a Y-shaped molecule.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Igarashi T,Sato M,Katsube Y,Takio K,Tanaka T,Nakanishi M,Arata Ydoi
10.1021/bi00476a013subject
Has Abstractpub_date
1990-06-19 00:00:00pages
5727-33issue
24eissn
0006-2960issn
1520-4995journal_volume
29pub_type
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