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대한생식의학회지 제21권 제1호 2010년

H-Y 항원의 정제 및 특성규명에 관한 연구

건국대학교 동물자원연구센터;건국대학교 동물자원연구센터;건국대학교 동물자원연구센터;건국대학교 동물자원연구센터;건국대학교 동물자원연구센터;건국대학교 동물자원연구센터;

정미경;백정미;이정열;허용수;김창규;김종배;,

Studies on the Purification and Characterization of H-Y Antigen

Chung, M.K.;Paik, J.M.;Lee, J.L.;Heo, Y.S.;Kim, C.K.;Kim, J.B.;

Animal Resources Resarch Center, Kon-Kuk University;Animal Resources Resarch Center, Kon-Kuk University;Animal Resources Resarch Center, Kon-Kuk University;Animal Resources Resarch Center, Kon-Kuk University;Animal Resources Resarch Center, Kon-Kuk University;Animal Resources Resarch Center, Kon-Kuk University;

These studies were carried out to investigate the properties of H-Y antigen purified by immunoaffinity chromatography using monoclonal H-Y antibody. Immunoaffinity column was prepared by the coupling of monoclonal antibody to the Aminolink Coupling Gel. Murine testis supernatant was applied onto the column and eluted by O.lM glycine-HCl buffer and 31${\mu}g$ of H-Y Ag was eluted from one testis. Purified H-Y Ag strongly reacted with Con A and lentil from 6 different kinds of lectins tested, which may indicate that sugar moiety of H-Y Ag is composed of glucose, mannose and their derivatives. Con A-sepharose affinity column was used to purified H-Y Ag based on that H-Y Ag is glycoprotein. The fraction eluted by 0.2M Me-${\alpha}$-D-mannoside from the column loaded with murine testis supernatant was identified to be H-Y Ag by dot blot test. Molecular weight of the purified H-Y Ag was estimated by Sepharose G-75 gel filtration and SDS-PAGE, and showing that it was about 67,000 dalton. In fluorescence test, the ratio of XY embryos and XX embryos was 1:1.

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