Mechanisms of generation of antibody diversity as a cause for natural selection of homoiothermal animals in the process of evolution.

The temperature-dependence of domain interactions in the Fab, Fc, Fb and Fv fragments from human myeloma immunoglobulins (IgG) samples was investigated by scanning microcalorimetry, NMR and difference spectroscopy. The fragments were found to be very sensitive to temperature changes. Lowering the temperature below the physiological value (37 degrees C) considerably decreases the energy of interaction of the variable VH and VL domains, resulting at times in their dissociation.

Nucleotide sequence of the Yersinia pestis gene encoding F1 antigen and the primary structure of the protein. Putative T and B cell epitopes.

The plasmid-located gene caf1 encoding the capsular antigen fraction 1 (F1) of Yersinia pestis was cloned and sequenced. The gene codes for a 170 amino acid peptide with a deduced Mr of 17.6 kDa.

Peculiar features of application of pH gradients formed in borate buffer with a polyhydroxy compound for separation of proteins in a free-flow electrophoretic apparatus.

The use of pH gradients in borate buffer with a polyhydroxy compound for separation of proteins in a free-flow electrophoretic apparatus is outlined. The composition of the pH gradients, the free-flow apparatus design and its operation, and the main causes of failures in the protein separation are considered.