| Autor: |
Jiro Arima, Yuto Sakate, Keigo Monden, Hiroki Kobayashi, Michika Nishi, Katsuhiko Shimizu |
| Rok vydání: |
2022 |
| Předmět: |
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| Zdroj: |
Journal of Bioscience and Bioengineering. 134:477-483 |
| ISSN: |
1389-1723 |
| DOI: |
10.1016/j.jbiosc.2022.09.001 |
| Popis: |
Glassin is a water-soluble protein from the siliceous skeleton of a marine sponge that adsorbs tightly to silica at pH 7.0-9.0 and accelerates silica particle formation from silicic acid. Glassin comprises three distinct domains: a His and Asp-rich (HD) domain, a Pro-rich (P) domain, and a His and Thr-rich (HT) domain. Here, we investigated the roles of these three domains in silica adsorption by using glutathione S-transferase (GST) fused with glassin or with each domain. GST fused with the HD domain exhibited tight adsorption, equivalent to that of GST fused with the full-length glassin sequence at values above 7.0. The apparent K |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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