Modification of thyroxine-binding globulin with p -iodophenylsulfonyl (pipsyl) chloride and effect on thyroxine binding activity
| Autor: | Jessie Shih Siegel, Milton Tabachnick, Ladislav Korcek |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
Globulin
Biophysics Sulfur Radioisotopes Biochemistry Chloride Thyroxine-Binding Proteins Residue (chemistry) chemistry.chemical_compound Thyroxine-binding globulin Structural Biology Mole Genetics medicine Humans Sulfones Derivatization Molecular Biology biology Iodobenzenes Chemistry Cell Biology Transport protein Kinetics Thyroxine Reagent biology.protein Serum Globulins medicine.drug |
| Zdroj: | FEBS Letters. 102:306-310 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(79)80024-1 |
| Popis: | Thyroxine-binding globulin (TBG) is the major transport protein of the thyroid hormones in human plasma. As part of a study of the chemistry of the thyroxine binding site on TBG, we have been investigating a series of protein modifying reagents for their effect on thyroxine binding. Among the reagents assayed, p-iodophenylsulfonyl (pipsyl) chloride proved to be of interest, since relatively low levels of protein modification with this reagent resulted in concomitant decreases in thyroxine binding activity. The present communication describes the results of an investigation involving the effect of derivatization of TBG with pipsyl chloride on the thyroxine binding activity of the protein. The results indicate that there is a direct relationship between the degree of pipsylation and the percent decrease in thyroxine binding activity at relatively low levels of pipsyl group incorporated per mole protein. Analyses of hydrolyzates of pipsylated TBG preparations modified with [35S]pipsyl chloride, indicate that the principal group derivatized in TBG is an e-amino group of a specific lysyl residue probably located near the thyroxine binding site. |
| Databáze: | OpenAIRE |
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