Expression and purification of murine ?-1,3-galactosyltransferase catalytic domain / 中国免疫学杂志
Chinese Journal of Immunology
; (12)1985.
Article
en Zh
| WPRIM
| ID: wpr-544612
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WPRO
ABSTRACT
Objective:To express and purificate catalytic domain of murine?-1,3-galactosyltransferase and provide the feasible method in the tumor cell surface production ?-gal epitopes..Methods:This research established expression system in pET-15b to express catalytic domain of murine ?-1,3-galactosyltransferase,then identified its activity by HPLC with anion exchange column.Results:(1)Constructed successfully recombinant ?-1,3-galactosyltransferase catalytic domain with His-tag.(2)?-1,3-galactosyltransferase with His-tag in a soluble form was expressed and purificated effeciently.(3)Its activity by HPLC with anion exchange column showed.Conclusion:This research shows ?-1,3-galactosyltransferase in a soluble form has been expressed successfully.
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WPRIM
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Zh
Revista:
Chinese Journal of Immunology
Año:
1985
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Article