title: Development of a purification procedure for the placental protein 14 involving metal-chelate affinity chromatography and hydrophobic interaction chromatography.
abstract: 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.
authors.affiliation: Hematological Scientific Center, Russian Academy of Medical Science, Moscow.
authors.forename: A L
authors.initials: AL
authors.lastname: Berkovsky
authors.forename: P P
authors.initials: PP
authors.lastname: Potapov
mesh_terms: 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*
chemical_list: D002614:Chelating Agents; D000071816:Glycodelin; D006023:Glycoproteins; D008670:Metals; C045246:PAEP protein, human; D011257:Pregnancy Proteins