Keywords

Chicken Embryo, Tissue Membrane Protein, Mycoplasma Gallisepticum Adhesion Protein, Dot-Elisa

Abstract

Using the pgex fusion protein expression system, the coding sequences of Mycoplasma gallisepticum adhesion protein (pmga) and gst were fused and expressed in Escherichia coli bl21. After purification by gst¡¤bindresin, the purity of gst-pmga reached 96%. Using protease thrombin to cut off the GST tag, pmga with a purity of 96% was obtained, which was identified by western-blot as having good immunological activity. The tissue membrane proteins of the trachea, heart, liver, lungs, kidneys, glandular stomach, duodenum, bursa of Fabricius, thymus and spleen of spf chicken embryos were extracted by differential centrifugation, and the dot enzyme-linked immunosorbent assay (dot- elisa) to detect the binding of membrane proteins of various tissues to PMGA. The results showed that, except for the spleen, there was specific binding between the membrane proteins of other tissues and pmga, indicating that there were pmga receptor proteins in the membrane proteins of these tissues. After sds-page analysis, it was found that except for the spleen, the membrane proteins of the other nine tissues contain a main band with a relative molecular mass of about 30ku. The relative molecular mass of the receptor may be 30ku, which can provide a basis for in-depth study of PMGA receptors. Protein provides information.

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Original research done by Peng Xiuli, Gao Junwei, Hu Sishun, Hu Fuli, Bi Dingren

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