Tyrosine Sulfation of Statherin
Tyrosylprotein sulfotransferase (TPST), responsible for the sulfation of a variety of secretory and membrane proteins, has been identified and characterized in submandibular salivary glands (William et al. Arch Biochem Biophys 1997; 338: 90-96). In the present study we demonstrate the sulfation of a...
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Ivyspring International Publisher
2007
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1820877/ |
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pubmed-18208772007-03-27 Tyrosine Sulfation of Statherin Kasinathan, C. Gandhi, N. Ramaprasad, P. Sundaram, P. Ramasubbu, N. Research Paper Tyrosylprotein sulfotransferase (TPST), responsible for the sulfation of a variety of secretory and membrane proteins, has been identified and characterized in submandibular salivary glands (William et al. Arch Biochem Biophys 1997; 338: 90-96). In the present study we demonstrate the sulfation of a salivary secretory protein, statherin, by the tyrosylprotein sulfotransferase present in human saliva. Optimum statherin sulfation was observed at pH 6.5 and at 20 mm MnCl2. Increase in the level of total sulfation was observed with increasing statherin concentration. The Kmvalue of tyrosylprotein sulfotransferase for statherin was 40 μM. Analysis of the sulfated statherin product on SDS-polyacrylamide gel electrophoresis followed by autoradiography revealed 35S-labelling of a 5 kDa statherin. Further analysis of the sulfated statherin revealed the sulfation on tyrosyl residue. This study is the first report demonstrating tyrosine sulfation of a salivary secretory protein. The implications of this sulfation of statherin in hydroxyapatite binding and Actinomyces viscosus interactions are discussed. Ivyspring International Publisher 2007-03-02 /pmc/articles/PMC1820877/ /pubmed/17389930 Text en © Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Kasinathan, C. Gandhi, N. Ramaprasad, P. Sundaram, P. Ramasubbu, N. |
| spellingShingle |
Kasinathan, C. Gandhi, N. Ramaprasad, P. Sundaram, P. Ramasubbu, N. Tyrosine Sulfation of Statherin |
| author_facet |
Kasinathan, C. Gandhi, N. Ramaprasad, P. Sundaram, P. Ramasubbu, N. |
| author_sort |
Kasinathan, C. |
| title |
Tyrosine Sulfation of Statherin |
| title_short |
Tyrosine Sulfation of Statherin |
| title_full |
Tyrosine Sulfation of Statherin |
| title_fullStr |
Tyrosine Sulfation of Statherin |
| title_full_unstemmed |
Tyrosine Sulfation of Statherin |
| title_sort |
tyrosine sulfation of statherin |
| description |
Tyrosylprotein sulfotransferase (TPST), responsible for the sulfation of a variety of secretory and membrane proteins, has been identified and characterized in submandibular salivary glands (William et al. Arch Biochem Biophys 1997; 338: 90-96). In the present study we demonstrate the sulfation of a salivary secretory protein, statherin, by the tyrosylprotein sulfotransferase present in human saliva. Optimum statherin sulfation was observed at pH 6.5 and at 20 mm MnCl2. Increase in the level of total sulfation was observed with increasing statherin concentration. The Kmvalue of tyrosylprotein sulfotransferase for statherin was 40 μM. Analysis of the sulfated statherin product on SDS-polyacrylamide gel electrophoresis followed by autoradiography revealed 35S-labelling of a 5 kDa statherin. Further analysis of the sulfated statherin revealed the sulfation on tyrosyl residue. This study is the first report demonstrating tyrosine sulfation of a salivary secretory protein. The implications of this sulfation of statherin in hydroxyapatite binding and Actinomyces viscosus interactions are discussed. |
| publisher |
Ivyspring International Publisher |
| publishDate |
2007 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1820877/ |
| _version_ |
1611394961407737856 |