ABSTRACT
Human trophoblastic beta-glycoprotein (TBG) was subjected to immunoelectrophoresis with intermediate gel containing hormones. We have observed TBG binding either with cyclopentaneperhydrophenanthrene derivatives (cholesterol, testosterone, progesterone, estradiol, estrone) or their synthetic analogs (sinestrol, diethylstilbestrol). TGB showed markedly higher affinity to estrogens than to other hormones.
Subject(s)
Gonadal Steroid Hormones/metabolism , Hormones/metabolism , Pregnancy-Specific beta 1-Glycoproteins/metabolism , Cholesterol/metabolism , Drug Interactions , Female , Humans , Immunoelectrophoresis, Two-Dimensional , Male , Protein BindingABSTRACT
During immunoelectrophoresis in the presence of tween-80, triton X-100 and ammonium sulfate blood serum beta-glycoprotein of pregnant rats migrated along with beta-globulins as a main single band; its minor components in zones of alpha- and gamma-globulins were not detected. beta-glycoprotein was completely absorbed by phenyl sepharose in the absence of ligand as well as when the spacer arm for phenyl group was short. When the phenyl group was linked with the template through a long spacer arm, three froms of beta-glycoprotein with different immunoelectrophoretic mobility were detected after absorbtion with phenyl sepharose. Hence, beta-glycoprotein is hydrophobic and is represented by alpha-, beta- and gamma-forms in blood plasma of pregnant rats.
Subject(s)
Pregnancy Proteins/pharmacology , Pregnancy, Animal/blood , Pregnancy-Specific beta 1-Glycoproteins/pharmacology , Alpha-Globulins/analysis , Animals , Beta-Globulins/analysis , Chromatography, Affinity/methods , Female , Immunoelectrophoresis, Two-Dimensional/methods , Pregnancy , Pregnancy-Specific beta 1-Glycoproteins/analysis , Pregnancy-Specific beta 1-Glycoproteins/isolation & purification , Rats , gamma-Globulins/analysisABSTRACT
The pregnancy-specific beta 1-globulin (SBG) reacts with 10 out of 11 lectins which have affinity to monosaccharides (glucose, mannose, galactose and fucose) and acetylamino sugars. The affinity to ConA and PHA-P was the most pronounced while this protein did not react with the pea lectin. The SBG reactions are specific for every lectin (even with the identical carbohydrate specificity). Peculiarities of the SBG reactions with lectins made it possible to reveal a few forms of this protein which differ in the carbohydrate composition and conformation of carbohydrate radicals.
