Demonstration of two distinct insulin-binding components in solubilized human placental membranes by radioimmunoassay using synthetic peptide and anti-synthetic peptide antibody.
A peptide corresponding to the 957-980 sequence of human placental insulin receptor precursor (HIRP) was synthesized and antisera were produced against the synthetic peptide. Anti-synthetic HIRP(957-980) serum HIR-27 was proved to cross-react with HIRP-related proteins in solubilized human placental membranes. A radioimmunoassay developed with the antiserum and synthetic peptide HIRP(957-980) enabled us to separate, in combination with gel filtration, two insulin-binding components in solubilized human placental membranes which conceivably correspond to the alpha 2 beta 2 and alpha beta structures of the placental insulin receptor. The two components were shown to be distinct in insulin-binding behavior depending on conditions of pH and ionic strength in the binding assay.
Yanaihara
N
N
University of Shizuoka School of Pharmaceutical Sciences, Japan.
Yanaihara
C
C
Iguchi
K
K
Inoue
T
T
Toyoshige
M
M
Mochizuki
T
T
Hoshino
M
M
Kurokawa
N
N
Kaneko
T
T
D000906:Antibodies; D000936:Antigen-Antibody Complex; D002462:Cell Membrane / Q000378:metabolism; D005260:Female; D006801:Humans; D007106:Immune Sera; D007700:Kinetics; D010455:Peptides / Q000138:chemical synthesis*; D010920:Placenta / Q000378:metabolism*; D011247:Pregnancy; D011863:Radioimmunoassay / Q000379:methods; D011972:Receptor, Insulin / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism
D000906:Antibodies; D000936:Antigen-Antibody Complex; D007106:Immune Sera; D010455:Peptides; D011972:Receptor, Insulin