[Changes in the adiabatic compressibility of mono- and polyclonal antibodies during interaction with antigens].
The values of apparent adiabatic compressibility of free and antigen-bound antibodies were determined by means of precise density and ultrasound velocity measurements. It was shown that during the formation of soluble immune complexes (insulin--monoclonal antibodies to insulin and alpha-amylase--monovalent Fab-fragments of antibodies to alpha-amylase), the apparent compressibility of antibodies decreased by (0.3 divided by 0.9).10(-6) cm3/g.bar. During the formation of large insoluble aggregates (alpha-amylase--polyclonal antibodies to alpha-amylase), the apparent compressibility decreased by (5.5 +/- 0.7).10(-6) cm3/g.bar. It is suggested that the decrease in the magnitude of thermal fluctuations of the molecular volume of antibodies during antigen binding, manifesting itself by the decrease in their compressibility and strengthened several-fold by precipitate formation, may favour the activation of the effectory functions of antibodies.
A I
AI
Priev
A P
AP
Sarvazian
B B
BB
Dzantiev
A V
AV
Zherdev
T V
TV
Cherednikova
D000818:Animals; D000906:Antibodies / Q000378:metabolism*; D000911:Antibodies, Monoclonal / Q000378:metabolism*; D000937:Antigen-Antibody Reactions; D007140:Immunoglobulin Fab Fragments / Q000378:metabolism; D007330:Insulin Antibodies / Q000378:metabolism; D008954:Models, Biological; D013552:Swine; D013816:Thermodynamics; D000516:alpha-Amylases / Q000276:immunology
D000906:Antibodies; D000911:Antibodies, Monoclonal; D007140:Immunoglobulin Fab Fragments; D007330:Insulin Antibodies; D000516:alpha-Amylases
Izmenenie adiabaticheskoĭ szhimaemosti mono- i poliklonal'nykh antitel pri vzaimodeĭstvii s antigenami.