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Purification and general properties of δ-aminolaevulate dehydratase from cow liver
1. δ-Aminolaevulate dehydratase, the enzyme catalysing the condensation of δ-aminolaevulic acid to porphobilinogen, has been prepared from cow liver and its properties have been studied. The enzyme has been purified 310-fold. 2. The purified preparation behaves as a single protein under gel filtrati...
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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
1967
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1270567/ https://ncbi.nlm.nih.gov/pubmed/6035515 |
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