Журнал хроматографии и методов разделения
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Preparation of Universal Peroxidase-Labelled Bacterial Protein Conjugates and Separation Properties

Angel Alberto Justiz-Vaillant

The aim of this study was to produce chimeric bacterial protein conjugates, to separate them by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and study their reactivities with human serum immunoglobulins by immunoblot analysis. Universal conjugates: protein LA-peroxidase (SpLA-HRP), protein LG-peroxidase (SpLG-HRP), protein AG-peroxidase (SpAG-HRP), protein LAG-peroxidase (SpLAG-HRP) and others were prepared by the periodate method. The conjugates were polymeric, with high molecular weights (MW) ranging from between 80-90 kDa to greater than 220 kDa. All conjugates have similar numbers of protein bands. However SpLALG-HRP and SpLAG anti-IgY-HRP were less polymeric. Immunoblot blot analysis showed that all conjugates reacted with human serum Igs. These conjugates have a potential use in epidemiological surveys of zoonotic infections affecting avian and mammalian species.The periodate method was effective to producing chimeric conjugates of peroxidase-labelled immunoglobulin-binding proteins and the immunoblot analysis showed that they were funtional and effective in reacting with human serum immunoglobulins.