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. 1967 Feb;102(2):423–431. doi: 10.1042/bj1020423

Purification and properties of crystalline 3-hydroxybutyrate dehydrogenase from Rhodopseudomonas spheroides

H U Bergmeyer 1, K Gawehn 1, H Klotzsch 1, H A Krebs 1, D H Williamson 1
PMCID: PMC1270263  PMID: 4291491

Abstract

1. The purification and crystallization of 3-hydroxybutyrate dehydrogenase from extracts of Rhodopseudomonas spheroides is described. 2. The molecular weight was calculated to be 85000 by sedimentation equilibrium. 3. Although the enzyme is stable at 0–4°, dilute solutions are rapidly inactivated at 37°; NADH2 or Ca2+ ions prevent this inactivation. 4. The enzyme is extremely sensitive to mercurials, but can be protected by NADH2 or Ca2+ ions. 5. From studies on p-hydroxymercuribenzoate binding it is estimated that the enzyme contains 5–6 moles of rapidly reacting thiol groups/mole. 6. d-Lactate and dl-2-hydroxybutyrate are competitive inhibitors of d-3-hydroxybutyrate oxidation. 7. The properties of the crystalline enzyme are compared with those of 3-hydroxybutyrate dehydrogenase preparations from other sources.

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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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