Receptor binding and biological activity of [SerB24]-insulin, an abnormal mutant insulin.
[SerB24]-insulin, the second structurally abnormal mutant insulin, and [SerB25]-insulin were semisynthesized and were studied for receptor binding and biological activity. Receptor binding and biological activity determined by its ability to increase 2-deoxy-glucose uptake in rat adipocytes were 0.7-3% of native insulin for [SerB24]-insulin and 3-8% for [SerB25]-insulin. Negative cooperative effect of these analogues was also markedly decreased. Immunoreactivity of [SerB24]-insulin was decreased whereas that of [SerB25]-insulin was normal. Markedly decreased receptor binding of [SerB24]-insulin appeared to be due to substitution of hydrophobic amino acid, Phe, with a polar amino acid, Ser, at B24.
D000273:Adipose Tissue / Q000187:drug effects / Q000378:metabolism; D000818:Animals; D001667:Binding, Competitive; D003847:Deoxyglucose / Q000378:metabolism; D006801:Humans; D007328:Insulin / Q000031:analogs & derivatives* / Q000378:metabolism; D007700:Kinetics; D051381:Rats; D011972:Receptor, Insulin / Q000378:metabolism*
D007328:Insulin; C040795:insulin, Ser(B25)-; C040796:insulin, Ser(B24)-; D003847:Deoxyglucose; D011972:Receptor, Insulin