title: [Physico-chemical study of estrogen-binding alpha-globulin in humans].
abstract: Human estrogen-binding alpha-globulin (EBG) was shown to be a thermolabile glycoprotein with molecular mass of 290,000 daltons, its isoelectric point occurred at pI 6.02-6.04. The globulin was salted out with 50-70% of ammonium sulfate. Some organic and inorganic acids precipitated EBG. DNAase and RNAase did not affect the glycoprotein but trypsin hydrolyzed its molecule. The EBG preparation obtained may be used for production of monospecific antiserum in order to study the glycoprotein functions in a body.
mesh_terms: D002352:Carrier Proteins / Q000032:analysis*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006801:Humans; D007120:Immunochemistry; D011960:Receptors, Estrogen; D012738:Sex Hormone-Binding Globulin / Q000032:analysis*
chemical_list: D002352:Carrier Proteins; D011960:Receptors, Estrogen; D012738:Sex Hormone-Binding Globulin; C010140:estrophilin
vernacular_title: Fiziko-khimicheskoe izuchenie éstrogensviazyvaiushchego alpha-globulina cheloveka.