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Purification and general properties of δ-aminolaevulate dehydratase from Nicotiana tabacum L
1. δ-Aminolaevulate dehydratase (EC 4.2.1.24) was purified 80-fold from tobacco leaves and its properties were studied. 2. The enzyme had optimum pH7·4 in potassium phosphate buffer, K(m)6·25×10(−4)m at 37° and pH7·4, optimum temperature 45° and an activation energy of 11100 cal./mole. 3. The enzyme...
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| Main Authors: | , |
|---|---|
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
1969
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1184859/ https://ncbi.nlm.nih.gov/pubmed/4980718 |
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