Purification of pregnancy associated alpha 2 glyco protein in human serum

Hong K J.; Kim I S.; Jue D M.; Shim B S.

Korean Journal of Biochemistry 13(2): 105-114

1981


Accession: 006233406

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Abstract
Because of similarity of MW and electrophoretic mobility of pregnancy-associated .alpha.2-glycoprotein with haptoglobin polymeric forms (haptoglobin 2-1 and 2-2 types), purification of pregnancy-associated .alpha.2-glycoprotein is very difficult from sera of haptoglobin of polymeric forms. To settle the purification method of pregnancy-associated .alpha.2-glycoprotein, it was purified from pooled pregnant female sera containing haptoglobin polymeric forms by the following methods: DEAE-cellulose chromatography using 0.03 M acetate buffer, pH 4.7 (starting buffer) and 1 M sodium acetate (mixing buffer); starch block electrophoresis with barbital buffer (.mu. = 0.1), pH 8.6; gel filtration on Sephadex G-200 column, with 1 M Tris-HCl buffer containing 0.5 M NaCl; and refiltration. To remove haptoglobin polymers, the 1st step was performed in the specific condition that haptoglobins were selectively adsorbed, while pregnancy-associated .alpha.2-glycoprotein was not adsorbed.