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Pyridoxamine phosphate-oxidase and pyridoxal phosphate-phosphatase activities in Escherichia coli.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Turner, John M. Happold, F. Crossfield |
| Copyright Year | 1961 |
| Abstract | acetone), than found in earlier investigations. Mayer (1930) used a concentration of 66% for his determinations, but this is definitely inhibitory, though lese so for insoluble preparations than for soluble. The enzyme is remarkably stable before it becomes soluble and the activity of soluble preparations is retained well in the cold. The optimum temperature for enzyme action is much lower than for many enzymes, presumably because the temperature at which the enzyme is inactivated is comparatively low, particularly in the presence of acetone. The rise in chlorophyllase activity when darkgrown pea seedlings are transferred to light is similar to that found by Hageman & Arnon (1955) for triphosphopyridine nucleotide-linked glyceraldehyde phosphate dehydrogenase. Marcus (1960) induced the formation of triose phosphate dehydrogenase, without the development of chlorophyll, in kidney-bean leaves by brief exposure to red light. Booth (1960) found that a carotene-destroying enzyme system was not normally present in potatoes and carrots, but exposure to light leading to chlorophyll formation in the surface layers also caused the enzyme to appear. |
| File Format | PDF HTM / HTML |
| DOI | 10.1042/bj0780364 |
| Alternate Webpage(s) | http://www.biochemj.org/content/ppbiochemj/78/2/364.full.pdf |
| PubMed reference number | 13778735 |
| Alternate Webpage(s) | https://doi.org/10.1042/bj0780364 |
| Volume Number | 78 |
| Journal | The Biochemical journal |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
