Use of metal-chelate affinity chromatography and hydrophobic interaction chromatography for purification of placental protein 12.
Placental protein 12 was isolated from amniotic fluid. Albumin was removed by means of ion-exchange chromatography on DEAE-Sepharose and chromatography on Blue-Sepharose. Complete purification was obtained by metal-chelate affinity chromatography and hydrophobic interaction chromatography under mild conditions for desorption. Using this procedure large quantities of a highly purified preparation can be obtained in one run.
Berkovsky
A L
AL
Hematological Scientific Center, Russian Academy of Medical Science, Moscow.
Potapov
P P
PP
D000653:Amniotic Fluid / Q000737:chemistry; D002352:Carrier Proteins / Q000302:isolation & purification*; D002614:Chelating Agents; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D005260:Female; D006801:Humans; D005779:Immunodiffusion; D018970:Insulin-Like Growth Factor Binding Protein 1; D018969:Insulin-Like Growth Factor Binding Proteins; D011247:Pregnancy; D011257:Pregnancy Proteins / Q000302:isolation & purification*; D012685:Sepharose / Q000031:analogs & derivatives
D002352:Carrier Proteins; D002614:Chelating Agents; C032231:IGFBP1 protein, human; D018970:Insulin-Like Growth Factor Binding Protein 1; D018969:Insulin-Like Growth Factor Binding Proteins; D011257:Pregnancy Proteins; C029483:Blue-Sepharose; D012685:Sepharose