RESUMEN
A model involving quasicyclization of protein molecules following the stepwise reactions of limited proteolysis was developed. On the basis of the model new active sites were detected in immunoglobulins of various species as well as chemical synthesis of the sites was carried out. The new group of the substances was designated as immunopoietins. The primary structure of various species immunoglobulins was analyzed and evolutional stability of the immunopoietin structure was shown.
Asunto(s)
Fragmentos de Inmunoglobulinas/análisis , Inmunoglobulina G/análisis , Secuencia de Aminoácidos , Animales , Humanos , Especificidad de la Especie , Timopoyetinas/análisisRESUMEN
Conventional methods of peptide chemistry have been used to synthesize the C-terminal nonapeptide from human immunoglobulin E, which is a potential cytophilic binding site of the IgE molecule responsible for its primary recognition and binding to specific target cell receptors.
Asunto(s)
Inmunoglobulina E/síntesis química , Fragmentos de Inmunoglobulinas/síntesis química , Fragmentos de Péptidos/síntesis química , Secuencia de Aminoácidos , HumanosRESUMEN
Low-molecular fragments of immunoglobulins IgG-(245-349) (Glu-Pro-Gln-Val-Tyr), IgM-(451-455) (Arg-Pro-Asp-Val-Tyr), IgA-(347-351) (Arg-Pro-Glu-Val-His), and IgE-(430-435) (Ala-Ala-Pro-Glu-Val-Tyr), potentially active immunoregulators of a novel type, have been synthesised by classical methods of peptide chemistry. This group of compounds, which in biological effects are similar to thymopoietin, was given the name of immunopoietins.