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[Purification and physico-chemical characteristics of chorionic alpha1-microglobulin]
Abstract:
Highly purified chorionic alpha-microglobulin was isolated from amniotic fluid by precipitation with lantham chloride, ammonium and lithium sulfates coupled with adsorption chromatography with calcium pyrophosphate. The following physicochemical properties of the protein were determined: molecular weight, relative electrophoretic mobility, interaction with protamine sulfate and lectins, enzymatic stability and precipitation with salts.