Conformation of mucous glycoproteins in aqueous solvents
Shogren, R. L. ; Jamieson, A. M. ; Blackwell, J. ; Jentoft, N.
New York : Wiley-Blackwell
Published 1986
New York : Wiley-Blackwell
Published 1986
| ISSN: |
0006-3525
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|---|---|
| Keywords: |
Chemistry ; Polymer and Materials Science
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| Source: |
Wiley InterScience Backfile Collection 1832-2000
|
| Topics: |
Chemistry and Pharmacology
|
| Notes: |
Light-scattering techniques have been used to measure the z-average radius of gyration Rg z-average translational diffusion coefficient Dt and weight-average molecular weight Mw of porcine submaxillary mucin (PSM) in solution. PSM isolated at low shear in the presence of protease inhibitors has a Mw about twice as large as a sample prepared without these precautions. The former sample has a Mw of 17 × 106 in 0.1M NaCl, which decreases to 8 × 106 in 6M guanidine hydrochloride (GdnHCl) and then to 2 × 106 on addition of 0.1M mercaptoethanol to the 6M GdnHCl solution. The Rg or D-1t values obtained for PSM in this work superimpose with those of other authors for different mucin glycoproteins, leading to linear log-log relationships to the molecular weight of the protein core. Comparison of these results with those in the literature for denatured proteins suggest that mucins are linear random coils in which the protein core is stiffened by the presence of the oligosaccharide side chains. The length of the oligosaccharides and the nature of the solvent have little effect on the extension of the protein core. This suggests that the stiffness of the protein core is maintained by steric repulsion of the residues at the beginning of the oligosaccharide chains.
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| Additional Material: |
3 Ill.
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| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798297881665339392 |
|---|---|
| addmaterial | 3 Ill. |
| autor | Shogren, R. L. Jamieson, A. M. Blackwell, J. Jentoft, N. |
| autorsonst | Shogren, R. L. Jamieson, A. M. Blackwell, J. Jentoft, N. |
| book_url | http://dx.doi.org/10.1002/bip.360250809 |
| datenlieferant | nat_lic_papers |
| hauptsatz | hsatz_simple |
| identnr | NLM159575540 |
| iqvoc_descriptor_keyword | iqvoc_00000092:Materials |
| issn | 0006-3525 |
| journal_name | Biopolymers |
| materialart | 1 |
| notes | Light-scattering techniques have been used to measure the z-average radius of gyration Rg z-average translational diffusion coefficient Dt and weight-average molecular weight Mw of porcine submaxillary mucin (PSM) in solution. PSM isolated at low shear in the presence of protease inhibitors has a Mw about twice as large as a sample prepared without these precautions. The former sample has a Mw of 17 × 106 in 0.1M NaCl, which decreases to 8 × 106 in 6M guanidine hydrochloride (GdnHCl) and then to 2 × 106 on addition of 0.1M mercaptoethanol to the 6M GdnHCl solution. The Rg or D-1t values obtained for PSM in this work superimpose with those of other authors for different mucin glycoproteins, leading to linear log-log relationships to the molecular weight of the protein core. Comparison of these results with those in the literature for denatured proteins suggest that mucins are linear random coils in which the protein core is stiffened by the presence of the oligosaccharide side chains. The length of the oligosaccharides and the nature of the solvent have little effect on the extension of the protein core. This suggests that the stiffness of the protein core is maintained by steric repulsion of the residues at the beginning of the oligosaccharide chains. |
| package_name | Wiley-Blackwell |
| publikationsjahr_anzeige | 1986 |
| publikationsjahr_facette | 1986 |
| publikationsjahr_intervall | 8014:1985-1989 |
| publikationsjahr_sort | 1986 |
| publikationsort | New York |
| publisher | Wiley-Blackwell |
| reference | 25 (1986), S. 1505-1517 |
| schlagwort | Chemistry Polymer and Materials Science |
| search_space | articles |
| shingle_author_1 | Shogren, R. L. Jamieson, A. M. Blackwell, J. Jentoft, N. |
| shingle_author_2 | Shogren, R. L. Jamieson, A. M. Blackwell, J. Jentoft, N. |
| shingle_author_3 | Shogren, R. L. Jamieson, A. M. Blackwell, J. Jentoft, N. |
| shingle_author_4 | Shogren, R. L. Jamieson, A. M. Blackwell, J. Jentoft, N. |
| shingle_catch_all_1 | Shogren, R. L. Jamieson, A. M. Blackwell, J. Jentoft, N. Conformation of mucous glycoproteins in aqueous solvents Chemistry Polymer and Materials Science Chemistry Polymer and Materials Science Light-scattering techniques have been used to measure the z-average radius of gyration Rg z-average translational diffusion coefficient Dt and weight-average molecular weight Mw of porcine submaxillary mucin (PSM) in solution. PSM isolated at low shear in the presence of protease inhibitors has a Mw about twice as large as a sample prepared without these precautions. The former sample has a Mw of 17 × 106 in 0.1M NaCl, which decreases to 8 × 106 in 6M guanidine hydrochloride (GdnHCl) and then to 2 × 106 on addition of 0.1M mercaptoethanol to the 6M GdnHCl solution. The Rg or D-1t values obtained for PSM in this work superimpose with those of other authors for different mucin glycoproteins, leading to linear log-log relationships to the molecular weight of the protein core. Comparison of these results with those in the literature for denatured proteins suggest that mucins are linear random coils in which the protein core is stiffened by the presence of the oligosaccharide side chains. The length of the oligosaccharides and the nature of the solvent have little effect on the extension of the protein core. This suggests that the stiffness of the protein core is maintained by steric repulsion of the residues at the beginning of the oligosaccharide chains. 0006-3525 00063525 Wiley-Blackwell |
| shingle_catch_all_2 | Shogren, R. L. Jamieson, A. M. Blackwell, J. Jentoft, N. Conformation of mucous glycoproteins in aqueous solvents Chemistry Polymer and Materials Science Chemistry Polymer and Materials Science Light-scattering techniques have been used to measure the z-average radius of gyration Rg z-average translational diffusion coefficient Dt and weight-average molecular weight Mw of porcine submaxillary mucin (PSM) in solution. PSM isolated at low shear in the presence of protease inhibitors has a Mw about twice as large as a sample prepared without these precautions. The former sample has a Mw of 17 × 106 in 0.1M NaCl, which decreases to 8 × 106 in 6M guanidine hydrochloride (GdnHCl) and then to 2 × 106 on addition of 0.1M mercaptoethanol to the 6M GdnHCl solution. The Rg or D-1t values obtained for PSM in this work superimpose with those of other authors for different mucin glycoproteins, leading to linear log-log relationships to the molecular weight of the protein core. Comparison of these results with those in the literature for denatured proteins suggest that mucins are linear random coils in which the protein core is stiffened by the presence of the oligosaccharide side chains. The length of the oligosaccharides and the nature of the solvent have little effect on the extension of the protein core. This suggests that the stiffness of the protein core is maintained by steric repulsion of the residues at the beginning of the oligosaccharide chains. 0006-3525 00063525 Wiley-Blackwell |
| shingle_catch_all_3 | Shogren, R. L. Jamieson, A. M. Blackwell, J. Jentoft, N. Conformation of mucous glycoproteins in aqueous solvents Chemistry Polymer and Materials Science Chemistry Polymer and Materials Science Light-scattering techniques have been used to measure the z-average radius of gyration Rg z-average translational diffusion coefficient Dt and weight-average molecular weight Mw of porcine submaxillary mucin (PSM) in solution. PSM isolated at low shear in the presence of protease inhibitors has a Mw about twice as large as a sample prepared without these precautions. The former sample has a Mw of 17 × 106 in 0.1M NaCl, which decreases to 8 × 106 in 6M guanidine hydrochloride (GdnHCl) and then to 2 × 106 on addition of 0.1M mercaptoethanol to the 6M GdnHCl solution. The Rg or D-1t values obtained for PSM in this work superimpose with those of other authors for different mucin glycoproteins, leading to linear log-log relationships to the molecular weight of the protein core. Comparison of these results with those in the literature for denatured proteins suggest that mucins are linear random coils in which the protein core is stiffened by the presence of the oligosaccharide side chains. The length of the oligosaccharides and the nature of the solvent have little effect on the extension of the protein core. This suggests that the stiffness of the protein core is maintained by steric repulsion of the residues at the beginning of the oligosaccharide chains. 0006-3525 00063525 Wiley-Blackwell |
| shingle_catch_all_4 | Shogren, R. L. Jamieson, A. M. Blackwell, J. Jentoft, N. Conformation of mucous glycoproteins in aqueous solvents Chemistry Polymer and Materials Science Chemistry Polymer and Materials Science Light-scattering techniques have been used to measure the z-average radius of gyration Rg z-average translational diffusion coefficient Dt and weight-average molecular weight Mw of porcine submaxillary mucin (PSM) in solution. PSM isolated at low shear in the presence of protease inhibitors has a Mw about twice as large as a sample prepared without these precautions. The former sample has a Mw of 17 × 106 in 0.1M NaCl, which decreases to 8 × 106 in 6M guanidine hydrochloride (GdnHCl) and then to 2 × 106 on addition of 0.1M mercaptoethanol to the 6M GdnHCl solution. The Rg or D-1t values obtained for PSM in this work superimpose with those of other authors for different mucin glycoproteins, leading to linear log-log relationships to the molecular weight of the protein core. Comparison of these results with those in the literature for denatured proteins suggest that mucins are linear random coils in which the protein core is stiffened by the presence of the oligosaccharide side chains. The length of the oligosaccharides and the nature of the solvent have little effect on the extension of the protein core. This suggests that the stiffness of the protein core is maintained by steric repulsion of the residues at the beginning of the oligosaccharide chains. 0006-3525 00063525 Wiley-Blackwell |
| shingle_title_1 | Conformation of mucous glycoproteins in aqueous solvents |
| shingle_title_2 | Conformation of mucous glycoproteins in aqueous solvents |
| shingle_title_3 | Conformation of mucous glycoproteins in aqueous solvents |
| shingle_title_4 | Conformation of mucous glycoproteins in aqueous solvents |
| sigel_instance_filter | dkfz geomar wilbert ipn albert |
| source_archive | Wiley InterScience Backfile Collection 1832-2000 |
| timestamp | 2024-05-06T10:15:02.666Z |
| titel | Conformation of mucous glycoproteins in aqueous solvents |
| titel_suche | Conformation of mucous glycoproteins in aqueous solvents |
| topic | V |
| uid | nat_lic_papers_NLM159575540 |