Structural analysis of purified human tracheobronchial mucins
| ISSN: |
0006-3525
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|---|---|
| Keywords: |
Chemistry ; Polymer and Materials Science
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| Source: |
Wiley InterScience Backfile Collection 1832-2000
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| Topics: |
Chemistry and Pharmacology
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| Notes: |
Light scattering has been used to investigate the structure of human tracheobronchial mucin glycoproteins (HTBM) from the sputum of cystic fibrosis patients. The specimen was extracted using 6M guanidinium hydrochloride solution and fractionated by gel exclusion chromatography on Sephacryl S-1000. The fractionated HTBM was purified by density gradient ultracentrifugation. Purity of the resulting material was confirmed by SDS polyacrylamide gel electrophoresis and uv spectroscopy. Light scattering measurements on the fractionated mucins yield weight-average molecular weights Mw, and z-average radii of gyration Rg, z. The native cystic fibrosis HTBM consisted of a high molecular weight fraction with Mw = 9.3 × 106 daltons and a lower molecular weight fraction contanining partly degraded mucins. After reduction and carboxymethylation of the high molecular weight native fraction, the resulting material was separated into three pools with Mw values of 5.1 × 106, 1.6 × 106, and 400,000. The derived molecular weights for the protein cores Mp,w, and the experimental radii of gyration are found to be consistent with the Mp,w - Rg relation established previously for submaxillary, cervical, and gastric mucins. These results imply that HTBM has the same extended-coil conformation reported for other mucins and has a molecular structure consisting of subunits, linked into linear chains via covalent (disulfide) bonds.
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| Additional Material: |
7 Ill.
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| Type of Medium: |
Electronic Resource
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| URL: |
| _version_ | 1798297882106789888 |
|---|---|
| addmaterial | 7 Ill. |
| autor | Gupta, R. Jentoft, N. Jamieson, A. M. Blackwell, J. |
| autorsonst | Gupta, R. Jentoft, N. Jamieson, A. M. Blackwell, J. |
| book_url | http://dx.doi.org/10.1002/bip.360290207 |
| datenlieferant | nat_lic_papers |
| hauptsatz | hsatz_simple |
| identnr | NLM159581451 |
| iqvoc_descriptor_keyword | iqvoc_00000092:Materials |
| iqvoc_descriptor_title | iqvoc_00000708:analysis |
| issn | 0006-3525 |
| journal_name | Biopolymers |
| materialart | 1 |
| notes | Light scattering has been used to investigate the structure of human tracheobronchial mucin glycoproteins (HTBM) from the sputum of cystic fibrosis patients. The specimen was extracted using 6M guanidinium hydrochloride solution and fractionated by gel exclusion chromatography on Sephacryl S-1000. The fractionated HTBM was purified by density gradient ultracentrifugation. Purity of the resulting material was confirmed by SDS polyacrylamide gel electrophoresis and uv spectroscopy. Light scattering measurements on the fractionated mucins yield weight-average molecular weights Mw, and z-average radii of gyration Rg, z. The native cystic fibrosis HTBM consisted of a high molecular weight fraction with Mw = 9.3 × 106 daltons and a lower molecular weight fraction contanining partly degraded mucins. After reduction and carboxymethylation of the high molecular weight native fraction, the resulting material was separated into three pools with Mw values of 5.1 × 106, 1.6 × 106, and 400,000. The derived molecular weights for the protein cores Mp,w, and the experimental radii of gyration are found to be consistent with the Mp,w - Rg relation established previously for submaxillary, cervical, and gastric mucins. These results imply that HTBM has the same extended-coil conformation reported for other mucins and has a molecular structure consisting of subunits, linked into linear chains via covalent (disulfide) bonds. |
| package_name | Wiley-Blackwell |
| publikationsjahr_anzeige | 1990 |
| publikationsjahr_facette | 1990 |
| publikationsjahr_intervall | 8009:1990-1994 |
| publikationsjahr_sort | 1990 |
| publikationsort | New York |
| publisher | Wiley-Blackwell |
| reference | 29 (1990), S. 347-355 |
| schlagwort | Chemistry Polymer and Materials Science |
| search_space | articles |
| shingle_author_1 | Gupta, R. Jentoft, N. Jamieson, A. M. Blackwell, J. |
| shingle_author_2 | Gupta, R. Jentoft, N. Jamieson, A. M. Blackwell, J. |
| shingle_author_3 | Gupta, R. Jentoft, N. Jamieson, A. M. Blackwell, J. |
| shingle_author_4 | Gupta, R. Jentoft, N. Jamieson, A. M. Blackwell, J. |
| shingle_catch_all_1 | Gupta, R. Jentoft, N. Jamieson, A. M. Blackwell, J. Structural analysis of purified human tracheobronchial mucins Chemistry Polymer and Materials Science Chemistry Polymer and Materials Science Light scattering has been used to investigate the structure of human tracheobronchial mucin glycoproteins (HTBM) from the sputum of cystic fibrosis patients. The specimen was extracted using 6M guanidinium hydrochloride solution and fractionated by gel exclusion chromatography on Sephacryl S-1000. The fractionated HTBM was purified by density gradient ultracentrifugation. Purity of the resulting material was confirmed by SDS polyacrylamide gel electrophoresis and uv spectroscopy. Light scattering measurements on the fractionated mucins yield weight-average molecular weights Mw, and z-average radii of gyration Rg, z. The native cystic fibrosis HTBM consisted of a high molecular weight fraction with Mw = 9.3 × 106 daltons and a lower molecular weight fraction contanining partly degraded mucins. After reduction and carboxymethylation of the high molecular weight native fraction, the resulting material was separated into three pools with Mw values of 5.1 × 106, 1.6 × 106, and 400,000. The derived molecular weights for the protein cores Mp,w, and the experimental radii of gyration are found to be consistent with the Mp,w - Rg relation established previously for submaxillary, cervical, and gastric mucins. These results imply that HTBM has the same extended-coil conformation reported for other mucins and has a molecular structure consisting of subunits, linked into linear chains via covalent (disulfide) bonds. 0006-3525 00063525 Wiley-Blackwell |
| shingle_catch_all_2 | Gupta, R. Jentoft, N. Jamieson, A. M. Blackwell, J. Structural analysis of purified human tracheobronchial mucins Chemistry Polymer and Materials Science Chemistry Polymer and Materials Science Light scattering has been used to investigate the structure of human tracheobronchial mucin glycoproteins (HTBM) from the sputum of cystic fibrosis patients. The specimen was extracted using 6M guanidinium hydrochloride solution and fractionated by gel exclusion chromatography on Sephacryl S-1000. The fractionated HTBM was purified by density gradient ultracentrifugation. Purity of the resulting material was confirmed by SDS polyacrylamide gel electrophoresis and uv spectroscopy. Light scattering measurements on the fractionated mucins yield weight-average molecular weights Mw, and z-average radii of gyration Rg, z. The native cystic fibrosis HTBM consisted of a high molecular weight fraction with Mw = 9.3 × 106 daltons and a lower molecular weight fraction contanining partly degraded mucins. After reduction and carboxymethylation of the high molecular weight native fraction, the resulting material was separated into three pools with Mw values of 5.1 × 106, 1.6 × 106, and 400,000. The derived molecular weights for the protein cores Mp,w, and the experimental radii of gyration are found to be consistent with the Mp,w - Rg relation established previously for submaxillary, cervical, and gastric mucins. These results imply that HTBM has the same extended-coil conformation reported for other mucins and has a molecular structure consisting of subunits, linked into linear chains via covalent (disulfide) bonds. 0006-3525 00063525 Wiley-Blackwell |
| shingle_catch_all_3 | Gupta, R. Jentoft, N. Jamieson, A. M. Blackwell, J. Structural analysis of purified human tracheobronchial mucins Chemistry Polymer and Materials Science Chemistry Polymer and Materials Science Light scattering has been used to investigate the structure of human tracheobronchial mucin glycoproteins (HTBM) from the sputum of cystic fibrosis patients. The specimen was extracted using 6M guanidinium hydrochloride solution and fractionated by gel exclusion chromatography on Sephacryl S-1000. The fractionated HTBM was purified by density gradient ultracentrifugation. Purity of the resulting material was confirmed by SDS polyacrylamide gel electrophoresis and uv spectroscopy. Light scattering measurements on the fractionated mucins yield weight-average molecular weights Mw, and z-average radii of gyration Rg, z. The native cystic fibrosis HTBM consisted of a high molecular weight fraction with Mw = 9.3 × 106 daltons and a lower molecular weight fraction contanining partly degraded mucins. After reduction and carboxymethylation of the high molecular weight native fraction, the resulting material was separated into three pools with Mw values of 5.1 × 106, 1.6 × 106, and 400,000. The derived molecular weights for the protein cores Mp,w, and the experimental radii of gyration are found to be consistent with the Mp,w - Rg relation established previously for submaxillary, cervical, and gastric mucins. These results imply that HTBM has the same extended-coil conformation reported for other mucins and has a molecular structure consisting of subunits, linked into linear chains via covalent (disulfide) bonds. 0006-3525 00063525 Wiley-Blackwell |
| shingle_catch_all_4 | Gupta, R. Jentoft, N. Jamieson, A. M. Blackwell, J. Structural analysis of purified human tracheobronchial mucins Chemistry Polymer and Materials Science Chemistry Polymer and Materials Science Light scattering has been used to investigate the structure of human tracheobronchial mucin glycoproteins (HTBM) from the sputum of cystic fibrosis patients. The specimen was extracted using 6M guanidinium hydrochloride solution and fractionated by gel exclusion chromatography on Sephacryl S-1000. The fractionated HTBM was purified by density gradient ultracentrifugation. Purity of the resulting material was confirmed by SDS polyacrylamide gel electrophoresis and uv spectroscopy. Light scattering measurements on the fractionated mucins yield weight-average molecular weights Mw, and z-average radii of gyration Rg, z. The native cystic fibrosis HTBM consisted of a high molecular weight fraction with Mw = 9.3 × 106 daltons and a lower molecular weight fraction contanining partly degraded mucins. After reduction and carboxymethylation of the high molecular weight native fraction, the resulting material was separated into three pools with Mw values of 5.1 × 106, 1.6 × 106, and 400,000. The derived molecular weights for the protein cores Mp,w, and the experimental radii of gyration are found to be consistent with the Mp,w - Rg relation established previously for submaxillary, cervical, and gastric mucins. These results imply that HTBM has the same extended-coil conformation reported for other mucins and has a molecular structure consisting of subunits, linked into linear chains via covalent (disulfide) bonds. 0006-3525 00063525 Wiley-Blackwell |
| shingle_title_1 | Structural analysis of purified human tracheobronchial mucins |
| shingle_title_2 | Structural analysis of purified human tracheobronchial mucins |
| shingle_title_3 | Structural analysis of purified human tracheobronchial mucins |
| shingle_title_4 | Structural analysis of purified human tracheobronchial mucins |
| sigel_instance_filter | dkfz geomar wilbert ipn albert |
| source_archive | Wiley InterScience Backfile Collection 1832-2000 |
| timestamp | 2024-05-06T10:15:02.666Z |
| titel | Structural analysis of purified human tracheobronchial mucins |
| titel_suche | Structural analysis of purified human tracheobronchial mucins |
| topic | V |
| uid | nat_lic_papers_NLM159581451 |