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KMID : 0358219940210010089
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Korean Journal of Fertility and Sterility
1994 Volume.21 No. 1 p.89 ~ p.98
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Studies on the Purification and Characterization of H-Y Antigne
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정미경
백정미/이정열/허용수/김창규/김종배
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Abstract
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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 0.1M glycine-HCI buffer and 31μg 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-α-D-mannoside from the
column
loaded with murine testis supernatant was identified to be H-Y Ag by dot not 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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