Pilz, Ingrid;
Schwarz, Erika;
Durchschein, Werner;
Licht, Arieh;
Sela, Michael
Effect of Cleaving Interchain Disulfide Bridges on the Radius of Gyration and Maximum Length of Anti-Poly (D-Alanyl) Antibodies before and after Reaction with Tetraalanine Hapten
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Medientyp:
E-Artikel
Titel:
Effect of Cleaving Interchain Disulfide Bridges on the Radius of Gyration and Maximum Length of Anti-Poly (D-Alanyl) Antibodies before and after Reaction with Tetraalanine Hapten
Erschienen:
National Academy of Sciences of the United States of America, 1980
Erschienen in:Proceedings of the National Academy of Sciences of the United States of America
Sprache:
Englisch
ISSN:
0027-8424
Entstehung:
Anmerkungen:
Beschreibung:
<p>The small-angle x-ray scattering of solutions of rabbit IgG antibodies and their derivatives has been investigated. The reduction and alkylation of the native antibodies cause a small increase of the molecular parameters, indicating a limited expansion of the molecule. Binding of native anti-poly(D-alanyl) antibodies with hapten (80% saturation) causes a significant change of the quaternary structure, expressed by a decrease in the maximum diameter of about 2 nm, of the radius of gyration by 5.5%, and of the volume. The same antibodies, in which the single inter-heavy-chain disulfide bridge was opened by reduction and carboxamidomethylation, do not show any significant decrease in the overall molecular parameters upon reaction with hapten, except for a local structural change in a part of the molecule. These data lend further support to the notion that binding of hapten induces a conformational transition in its specific antibodies and suggest that the opening of the interchain disulfide bridges affects that transition. The dimensions of the intact antibodies calculated from measurements of small-angle x-ray scattering at low concentrations agree closely with those obtained from crystallographic studies.</p>