Loading...
Please wait, while we are loading the content...
Similar Documents
Studies on amino acid decarboxylases in Escherichia coli.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Lawson, Arnold Quinn, A. G. |
| Copyright Year | 1967 |
| Abstract | The isolation of highly active preparations of glutamate decarboxylase, arginine decarboxylase and histidine decarboxylase from Escherichia coli is described. These preparations showed strict specificity, and were in each case resolved into apo- and co-enzyme as shown by the significant restoration of activity that took place on addition of pyridoxal 5-phosphate. |
| Starting Page | 1 |
| Ending Page | 6 |
| Page Count | 6 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.biochemj.org/content/ppbiochemj/105/2/483.full.pdf |
| PubMed reference number | 4868874v1 |
| Volume Number | 105 |
| Issue Number | 2 |
| Journal | The Biochemical journal |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Amino Acids Arginine decarboxylase Carboxy-Lyases Glutamate Decarboxylase Glutamic Acid HDC gene Histidine Occur (action) Pyridoxal Phosphate Thioctic Acid |
| Content Type | Text |
| Resource Type | Article |