Abstract
Cell wall‐bound peroxidase isolated from tobacco leaf mesophll cell walls was found to consist of two isoenzymes (P1 and P2). Each exists in the form of a single subunit with the same molecular weight (35 000) as determined by Sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis. Both isoenzymes exhibited maximum activities at 70°. P1 increased to 265% and P2 to 140% of the activities assayed at 27°; below this temperature the two isoenzymes had the same specific activity. On hydrolysis, P1 showed a carbohydrate content of 26.22% when the monosaccharides were analyzed by gas liquid chromatography; P2 gave 21.45%.
| Original language | English |
|---|---|
| Pages (from-to) | 1-4 |
| Number of pages | 4 |
| Journal | International Journal of Peptide and Protein Research |
| Volume | 14 |
| Issue number | 1 |
| Publication status | Published - Jul 1979 |
| Externally published | Yes |
Keywords
- carbohydrate contents of isoperoxidases
- isoperoxidases
- peroxidases
- thermal activation
- tobacco leaf isoperoxidases
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