Biological activity of some insulin derivatives
Asja Šiševa, L Sirakov, Jiřina Slaninová, Tomislav Barth
Abstract
Asja Šiševa, L Sirakov, Jiřina Slaninová, Tomislav Barth
Abstract
The ability of insulin and some of its derivatives to compete with 125I-insulin for the binding site in the membrane fraction prepared from the mammary gland of lactating mice is reported. The binding affinity decreased in the following order: insulin desoctapeptide-insulin tert-butyloxycarbonyl3-insulin tert-butyloxycarbonyl2-desoctapeptide-insulin. Insulin hexamethyl ester and its desoctapeptide in concentrations 5.5 . 10-11 - 2 . 10-5 M did not inhibit the binding of 125I-insulin. The comparison of the ability to decrease the blood glucose level showed that tert-butyloxycarbonyl3-insulin had 5% of the activity of insulin and that the other derivatives had less than 0.5% of that of insulin.
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The ability of insulin and some of its derivatives to compete with 125I-insulin for the binding site in the membrane fraction prepared from the mammary gland of lactating mice is reported. The binding affinity decreased in the following order: insulin desoctapeptide-insulin tert-butyloxycarbonyl3-insulin tert-butyloxycarbonyl2-desoctapeptide-insulin. Insulin hexamethyl ester and its desoctapeptide in concentrations 5.5 . 10-11 - 2 . 10-5 M did not inhibit the binding of 125I-insulin. The comparison of the ability to decrease the blood glucose level showed that tert-butyloxycarbonyl3-insulin had 5% of the activity of insulin and that the other derivatives had less than 0.5% of that of insulin.
Key concepts: Insulin, Internal medicine, Chemistry, Endocrinology, Biology, Medicine