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. 1967 Jul;104(1):244–249. doi: 10.1042/bj1040244

Purification and general properties of δ-aminolaevulate dehydratase from cow liver

A M del C Batlle 1, A M Ferramola 1, M Grinstein 1
PMCID: PMC1270567  PMID: 6035515

Abstract

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 filtration on Sephadex and Bio-Gel columns; it migrates as a single band in disk and starch-gel electro-phoresis at different pH values and it sediments as a single symmetrical peak in the ultracentrifuge. 3. The pH optimum for the pure enzyme was 6·8, the Km at pH 6·8 and 38° was 1·5×10-4m, the isoelectric point was about pH 4·9 and the molecular weight was 140000±14000 by the gel-filtration method. Maximal enzyme activity was observed at 65°. 4. The presence of thiol groups in the enzyme system, essential for its activity, was indicated and the total number of thiol groups was determined. 5. After the first steps of purification the enzyme required cysteine or reduced glutathione for activity.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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