Voprosy meditsinskoi khimii (ISSN 0042-8809)

Physico-chemical study of estrogen-binding alpha-globulin in humans

   
Mis'kova V.I., Pchelkina Z.M., Terent'ev A.A., Tatarinov Iu.S.
PubMed Id: 3953002
Year: 1986 vol: 32  issue:1  pages: 103-104
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.
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Reference: Mis'kova V.I., Pchelkina Z.M., Terent'ev A.A., Tatarinov Iu.S., Physico-chemical study of estrogen-binding alpha-globulin in humans, Voprosy meditsinskoi khimii, 1986, vol: 32(1), 103-104.
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