Development of a purification procedure for the placental protein 14 involving metal-chelate affinity chromatography and hydrophobic interaction chromatography.
Placental protein 14 was isolated from the biological material of patients undergoing legal abortions. The major part of ballast protein was removed by ion-exchange chromatography on DEAE-Sepharose and CM-Sepharose. Albumin was separated by chromatography on Blue-Sepharose. Complete purification was obtained by metal-chelate affinity chromatography on Nickel-Chelate Sepharose and hydrophobic interaction chromatography on Phenyl-Sepharose and Octyl-Sepharose. The protein was not exposed to denaturing agents or extreme pH.
Berkovsky
A L
AL
Hematological Scientific Center, Russian Academy of Medical Science, Moscow.
Potapov
P P
PP
D000029:Abortion, Legal; D002614:Chelating Agents / Q000737:chemistry; D002846:Chromatography, Affinity / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D000071816:Glycodelin; D006023:Glycoproteins / Q000302:isolation & purification*; D006801:Humans; D008670:Metals / Q000737:chemistry; D011247:Pregnancy; D011257:Pregnancy Proteins / Q000302:isolation & purification*
D002614:Chelating Agents; D000071816:Glycodelin; D006023:Glycoproteins; D008670:Metals; C045246:PAEP protein, human; D011257:Pregnancy Proteins