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Cloning and Characterization of the IgA Fc Receptor from Swine
( Yumei Chen ),( Yunchao Liu ),( Gaiping Zhang ),( Hua Feng ),( Pengchao Ji ),( Guoqiang Wang ),( Chang Liu ),( Yapeng Song ),( Yunfang Su ),( Songlin Qiao ),( Aiping Wang ) 한국미생물 · 생명공학회 2016 Journal of microbiology and biotechnology Vol.26 No.12
The myeloid-specific IgA Fc receptor (FcαR) is a cell surface molecule on immunocytes that provides a fundamental connection between humoral and cellular immunity. In this study, the full-length cDNA sequence of swine FcαRI (swFcαRI) was isolated and characterized and found to contain a 792-base-pair open reading frame, encoding a 264-amino-acid transmembrane glycoprotein with a predicted molecular mass of 29.4 kDa. The swFcαRI shares high amino acid sequence homology (>50%) with its counterparts from cattle, seal, and horse. Rosetting analysis confirmed that COS-7 cells transfected with an swFcαRI expression plasmid was able to combine with chicken erythrocytes sensitized with porcine IgA, but not IgG.