H-Y 항원의 정제 및 특성규명에 관한 연구

Studies on the Purification and Characterization of H-Y Antigen

  • 정미경 (건국대학교 동물자원연구센터) ;
  • 백정미 (건국대학교 동물자원연구센터) ;
  • 이정열 (건국대학교 동물자원연구센터) ;
  • 허용수 (건국대학교 동물자원연구센터) ;
  • 김창규 (건국대학교 동물자원연구센터) ;
  • 김종배 (건국대학교 동물자원연구센터)
  • Chung, M.K. (Animal Resources Resarch Center, Kon-Kuk University) ;
  • Paik, J.M. (Animal Resources Resarch Center, Kon-Kuk University) ;
  • Lee, J.L. (Animal Resources Resarch Center, Kon-Kuk University) ;
  • Heo, Y.S. (Animal Resources Resarch Center, Kon-Kuk University) ;
  • Kim, C.K. (Animal Resources Resarch Center, Kon-Kuk University) ;
  • Kim, J.B. (Animal Resources Resarch Center, Kon-Kuk University)
  • 발행 : 1994.04.30

초록

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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