Fluorescence polarization analysis of various immunoglobulins Dependence of rotational relaxation time on protein concentration and on ability to precipitate with antigen
- 1 May 1978
- journal article
- Published by Wiley in FEBS Letters
- Vol. 89 (1) , 89-92
- https://doi.org/10.1016/0014-5793(78)80529-8
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Neutron small‐angle scattering study on two different precipitin types of pig Anti‐Dnp antibodiesFEBS Letters, 1977
- Crystallographic structure studies of an IgG molecule and an Fc fragmentNature, 1976
- Different types of precipitating antibodies in early and late porcine anti-dinitrophenyl seraImmunochemistry, 1974
- Properties of myeloma immunoglobulin E(Yu). Chemical, fluorescence polarisation and spin-labeled studiesImmunochemistry, 1973
- Increase of the rotational relaxation time of antibody molecule after complex formation with dansyl‐haptenFEBS Letters, 1972
- Segmental flexibility in an antibody moleculeJournal of Molecular Biology, 1970
- Strong evidence for the freedom of rotation of immunoglobulin G subunitsJournal of Molecular Biology, 1970
- Flexibility of immunoglobulin G molecules as established by fluorescent polarisation measurementsImmunochemistry, 1969
- Fluorescence depolarization of rabbit gamma globulin conjugatesJournal of Molecular Biology, 1967
- IMMUNOLOGICAL STUDIES OF HUMAN γ-GLOBULINThe Journal of Experimental Medicine, 1960