Affinity labeling of human serum thyroxine-binding globulin with N-bromoacetyl-l-thyroxine: Identification of the labeled amino acid residues
| ISSN: |
0003-9861
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|---|---|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
|
| Topics: |
Biology
Chemistry and Pharmacology
Physics
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798292188548825088 |
|---|---|
| autor | Erard, F. Cheng, S.-Y. Robbins, J. |
| autorsonst | Erard, F. Cheng, S.-Y. Robbins, J. |
| book_url | http://dx.doi.org/10.1016/0003-9861(81)90060-6 |
| datenlieferant | nat_lic_papers |
| fussnote | The l-thyroxine binding site in human serum thyroxine-binding globulin was investigated by affinity labeling with N-bromoacetyl-l-thyroxine (BrAcT"4). Competitive binding studies showed that, in the presence of 100 molar excess of BrAcT"4, binding of thyroxine to thyroxine-binding globulin was nearly totally abolished. The reaction of BrAcT"4 to form covalent binding was inhibited in the presence of thyroxine and the affinity-labeled thyroxinebinding globulin lost its ability to bind thyroxine. These results indicate BrAcT"4 and thyroxine competed for the same binding site. Affinity labeling with 2 mol of BrAcT"4/mol of thyroxine-binding globulin resulted in the covalent attachment of 0.7 mol of ligand. By amino acid analysis and high voltage paper electrophoresis, methionine was identified as the major residue labeled (75%). Lysine, tyrosine, and histidine were also found to be labeled to the extent of 8, 8, and 5%, respectively. |
| hauptsatz | hsatz_simple |
| identnr | NLZ183368045 |
| issn | 0003-9861 |
| journal_name | Archives of Biochemistry and Biophysics |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 206 (1981), S. 15-20 |
| search_space | articles |
| shingle_author_1 | Erard, F. Cheng, S.-Y. Robbins, J. |
| shingle_author_2 | Erard, F. Cheng, S.-Y. Robbins, J. |
| shingle_author_3 | Erard, F. Cheng, S.-Y. Robbins, J. |
| shingle_author_4 | Erard, F. Cheng, S.-Y. Robbins, J. |
| shingle_catch_all_1 | Erard, F. Cheng, S.-Y. Robbins, J. Affinity labeling of human serum thyroxine-binding globulin with N-bromoacetyl-l-thyroxine: Identification of the labeled amino acid residues 0003-9861 00039861 Elsevier |
| shingle_catch_all_2 | Erard, F. Cheng, S.-Y. Robbins, J. Affinity labeling of human serum thyroxine-binding globulin with N-bromoacetyl-l-thyroxine: Identification of the labeled amino acid residues 0003-9861 00039861 Elsevier |
| shingle_catch_all_3 | Erard, F. Cheng, S.-Y. Robbins, J. Affinity labeling of human serum thyroxine-binding globulin with N-bromoacetyl-l-thyroxine: Identification of the labeled amino acid residues 0003-9861 00039861 Elsevier |
| shingle_catch_all_4 | Erard, F. Cheng, S.-Y. Robbins, J. Affinity labeling of human serum thyroxine-binding globulin with N-bromoacetyl-l-thyroxine: Identification of the labeled amino acid residues 0003-9861 00039861 Elsevier |
| shingle_title_1 | Affinity labeling of human serum thyroxine-binding globulin with N-bromoacetyl-l-thyroxine: Identification of the labeled amino acid residues |
| shingle_title_2 | Affinity labeling of human serum thyroxine-binding globulin with N-bromoacetyl-l-thyroxine: Identification of the labeled amino acid residues |
| shingle_title_3 | Affinity labeling of human serum thyroxine-binding globulin with N-bromoacetyl-l-thyroxine: Identification of the labeled amino acid residues |
| shingle_title_4 | Affinity labeling of human serum thyroxine-binding globulin with N-bromoacetyl-l-thyroxine: Identification of the labeled amino acid residues |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:44:33.428Z |
| titel | Affinity labeling of human serum thyroxine-binding globulin with N-bromoacetyl-l-thyroxine: Identification of the labeled amino acid residues |
| titel_suche | Affinity labeling of human serum thyroxine-binding globulin with N-bromoacetyl-l-thyroxine: Identification of the labeled amino acid residues The l-thyroxine binding site in human serum thyroxine-binding globulin was investigated by affinity labeling with N-bromoacetyl-l-thyroxine (BrAcT"4). Competitive binding studies showed that, in the presence of 100 molar excess of BrAcT"4, binding of thyroxine to thyroxine-binding globulin was nearly totally abolished. The reaction of BrAcT"4 to form covalent binding was inhibited in the presence of thyroxine and the affinity-labeled thyroxinebinding globulin lost its ability to bind thyroxine. These results indicate BrAcT"4 and thyroxine competed for the same binding site. Affinity labeling with 2 mol of BrAcT"4/mol of thyroxine-binding globulin resulted in the covalent attachment of 0.7 mol of ligand. By amino acid analysis and high voltage paper electrophoresis, methionine was identified as the major residue labeled (75%). Lysine, tyrosine, and histidine were also found to be labeled to the extent of 8, 8, and 5%, respectively. |
| topic | W V U |
| uid | nat_lic_papers_NLZ183368045 |