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Studies on Proteinases fromGliocladium roseum
| Content Provider | Scilit |
|---|---|
| Author | Kishida, Tadaaki Yoshimura, Sadahiko |
| Copyright Year | 1966 |
| Description | The alkaline proteinases of Gliocladium roseum (Link) Bainier were purified in crystalline forms by procedures of alcoholic precipitation, fuller's earth- and acrinol-treatment, and isolated in two types. (Proteinases I and II). Both of these proteinases were homogeneous on zone electrophoresis with polyacrylamide gel (Gyanogum 41), and had the optimal pH values of 11 (Proteinase I) and 10 (Proteinase II), and the optimal temperature of 45°C. The enzymatic reaction of proteinase I was remarkably promoted by $Fe^{++}$ and $Co^{++}$, and that of proteinase II was promoted by $Fe^{++}$, $Go^{++}$ and $Ca^{++}$, and both proteinases were protected from heat-inactivation by $Ca^{++}$ Proteinase II was activated remarkably by $Cl^{‒}$ under the existence of $Fe^{++}$, but proteinase I was unaffected by the anion. The order of strength of proteolytic power of these proteinases and chymotrypsin on casein was as follows; proteinase I> proteinase II> chymotrypsin. |
| Related Links | https://www.tandfonline.com/doi/pdf/10.1080/00021369.1966.10858749?needAccess=true |
| Ending Page | 1190 |
| Page Count | 8 |
| Starting Page | 1183 |
| ISSN | 09168451 |
| e-ISSN | 13476947 |
| DOI | 10.1080/00021369.1966.10858749 |
| Journal | Bioscience, Biotechnology, and Biochemistry |
| Issue Number | 12 |
| Volume Number | 30 |
| Language | English |
| Publisher | Informa UK Limited |
| Publisher Date | 1966-12-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Bioscience, Biotechnology, and Biochemistry Paper and Wood Treatment Electrophoresis Casein Optimal Alcoholic Proteinase Proteolytic Chymotrypsin Roseum Bainier |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Medicine Analytical Chemistry Molecular Biology Biochemistry Applied Microbiology and Biotechnology Biotechnology |
