ISSN:
1435-1536
Keywords:
Immunglobulin
;
conformation
;
X-ray
;
electronmicroscopy
;
neutron scattering
;
contrast variation
;
model computation
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
,
Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
Notes:
Summary Different experimental methods - hydrodynamical measurements, electronmicroscopy, X-ray crystallography, Yray and neutron small-angle scattering — provide data on the shape and dimensions of immunoglobulin molecules. Comparison of these data using model computation shows that the shape ofIgG immunoglobulin in dissolved state differs from that in crystalline state. The same statement is valid for the shape ofFab andFc fragments. Immunoglobulins of different origin have different dimensions. Correlation between the number of interchain disulphide bonds and the values of the radius of gyration may be observed. The value of the radius of gyration decreases when theIgG molecule binds haptens while the shape of the molecule seems to remain unchanged. This effect has a nonlinear dependence on the saturation of binding sites and may be connected with the effector function ofIgG molecule.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01525028
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