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G A Kozliaeva

Publications and source records attributed to G A Kozliaeva.

8 recordsLinked to original sources
PubMed1980

[Purification and physico-chemical characteristics of chorionic alpha1-microglobulin].

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.

Alpha-Globulins↗
PubMedDate not supplied

[Preparative isolation of human chorionic alpha 2-microglobulin].

A method is developed for isolation at the preparative scale of chorionic alpha 2-microglobulin from extracts of placenta of the first trimester of pregnancy using absorption chromatography on silica gel and aluminium hydrophosphate. Yield of the placenta protein was equal to 24% and the purity of the preparation obtained was about 90%.

Adsorption↗
PubMedDate not supplied

[Isolation of placental proteins by means of combined use of adsorption chromatography and immunochemical analysis].

Absorption chromatography was used to isolate antigens from placenta; the most effective purification of the antigens was achieved by selection of suitable eluents. Combined use of adsorption chromatography and immunochemical analyses showed that chorionic alpha1-globulin was isolated most effectively by means of calcium pyrophosphate and placental lactogen on the columns with silica gel and aluminum hydroxide.

Antigens↗
PubMedDate not supplied

[Isolation and purification of specific beta1-G-globulin].

Antigen, specific for trophoblastic tumor, was isolated from retroplacental blood by means of ion exchange chromatography on DEAE cellulose, gel filtration on Sephadex G-200, chromatography on hydroxylapatite and CM-cellulose and by preparative isofocusing using ampholines. Distinct heterogeneity of the protein and alteration in several its properties were observed as purity of the preparation was increased in course of isolation. A series of the protein preparations was obtained with 90-95% purity and with similar immunologic properties but the preparations differed in electrophoretic mobility, isoelectric points and some other patterns.

Animals↗