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Isolation and characterization of glyoxylate dehydrogenase from the fungus Sclerotium rolfsii.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Balmforth, Anthony J. Thomson, Andrew |
| Copyright Year | 1984 |
| Abstract | Glyoxylate dehydrogenase (glyoxylate:NAD+ oxidoreductase) was purified 600-fold in three steps from crude extracts of the fungus Sclerotium rolfsii (Corticium rolfsii Curzi). Two of the purification steps involved dye-affinity chromatography. The enzyme is a tetramer of Mr 250 000, with identical subunits of Mr 57 000. Inhibition studies suggest that there is one essential thiol group per active site. |
| Starting Page | 2970 |
| Ending Page | 2973 |
| Page Count | 4 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.biochemj.org/content/ppbiochemj/218/1/113.full.pdf |
| PubMed reference number | 6712607v1 |
| Volume Number | 218 |
| Issue Number | 1 |
| Journal | The Biochemical journal |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Athelia rolfsii Chromatography, Affinity Deficiency of glucose-6-phosphate dehydrogenase Dyes Fungi Glyoxylates Nicotinamide adenine dinucleotide (NAD) Sulfhydryl Compounds glyoxylate dehydrogenase (acylating) |
| Content Type | Text |
| Resource Type | Article |