A transcortin-binding protein in the plasma membrane of human syncytiotrophoblast.
Using affinity chromatography on immobilized transcortin of 125I-labeled, cholate-solubilized plasma membranes of human syncytiotrophoblast, a transcortin-binding protein with a minimal Mr of about 20 kDa has been isolated. It was found to be a sialoglycoprotein with an isoelectric point at pH 4.4 (about 5.0 after the treatment with neuraminidase). We assume that this protein is a component of membrane recognition system for transcortin-steroid complexes.
Krupenko
S A
SA
Institute of Bioorganic Chemistry, Byelorussian Academy of Sciences, Minsk, U.S.S.R.
Avvakumov
G V
GV
Strel'chyonok
O A
OA
D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D011232:Chemical Precipitation; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007525:Isoelectric Focusing; D011956:Receptors, Cell Surface / Q000302:isolation & purification*; D011987:Receptors, Steroid / Q000302:isolation & purification*; D015843:Serpins; D014156:Transcortin / Q000378:metabolism*; D014238:Trichloroacetic Acid; D014327:Trophoblasts / Q000737:chemistry / Q000378:metabolism*
D011956:Receptors, Cell Surface; D011987:Receptors, Steroid; C534935:SERPINA6 protein, human; D015843:Serpins; D014238:Trichloroacetic Acid; D014156:Transcortin