Steroidumwandelnde Enzyme aus Mikroorganismen X. Anreicherung einer 4-En-3-oxosteroid-5α-Reduktase ausMycobacterium smegmatis sowie Abtrennung und Anreicherung des Apoenzyms mit Hilfe der Affinitätschromatographie

Atrat, P.; Deppmeyer, V.; Groh, H.; Hörhold, C.

doi:10.1002/jobm.3630190602

Cited by 3 publications

References 5 publications

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Steroidumwandelnde Enzyme aus Mikroorganismen IX. Affinitätschromatographische Präparation und Untersuchung des Apoenzyms einer 4‐En‐3‐oxosteroid: (Akzeptor)‐1‐en‐oxidoreduktase aus Nocardia opaca

Atrat

Deppmeyer

Hörhold

et al. 1979

J of Basic Microbiology

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prosthetic group and apoenzyme were separated quantitatively by means of affinity chromatography in the presence of 2 M (NH,),SO, at p H 3.0. Subsequently the apoenzyme was eluted from affinity matrix by 0.01 M phosphate buffer, pH 8.0, whereas under these conditions the intact enzyme could not be eluted. The whole enzyme activity applied could be restored by incubation of the eluted apoenzyme with FAD. The binding strength of the apoenzyme to the immobilized steroid ligand is highly decreased in comparison to the native enzyme and can be interpreted by the action of rest hydrophobicity. That indicates the essential character of FAD for both ligand binding and transformation.

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Steroidumwandelnde Enzyme aus Mikroorganismen IX. Affinitätschromatographische Präparation und Untersuchung des Apoenzyms einer 4‐En‐3‐oxosteroid: (Akzeptor)‐1‐en‐oxidoreduktase aus Nocardia opaca

Atrat

Deppmeyer

Hörhold

et al. 1979

J of Basic Microbiology

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Steroidumwandelnde Enzyme aus Mikroorganismen IX. Affinitätschromatographische Präparation und Untersuchung des Apoenzyms einer 4-En-3-oxosteroid: (Akzeptor)-1-en-oxidoreduktase ausNocardia opaca

Atrat¹,

Deppmeyer²,

Hörhold³

et al. 1979

Z Allg Mikrobiol

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From the flavoenzyme, 4-en-3-oxosteroid: (acceptor)-1-en-oxidoreductase of Nocardia opaca, prosthetic group and apoenzyme were separated quantitatively by means of affinity chromatography in the presence of 2 M (NH4)2 at pH 3.0. Subsequently the apoenzyme was eluted from affinity matrix by 0.01 M phosphate buffer, pH 8.0, whereas under these conditions the intact enzyme could not be eluted. The whole enzyme activity applied could be restored by incubation of the eluted apoenzyme with FAD. The binding strength of the apoenzyme to the immobilized steroid ligand is highly decreased in comparison to the native enzyme and can be interpreted by the action of rest hydrophobicity. That indicates the essential character of FAD for both ligand binding and transformation.

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Recombinant DNA Technology

Malik

1981

Advances in Applied Microbiology

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Steroidumwandelnde Enzyme aus Mikroorganismen X. Anreicherung einer 4-En-3-oxosteroid-5α-Reduktase ausMycobacterium smegmatis sowie Abtrennung und Anreicherung des Apoenzyms mit Hilfe der Affinitätschromatographie

Cited by 3 publications

References 5 publications

Steroidumwandelnde Enzyme aus Mikroorganismen IX. Affinitätschromatographische Präparation und Untersuchung des Apoenzyms einer 4‐En‐3‐oxosteroid: (Akzeptor)‐1‐en‐oxidoreduktase aus Nocardia opaca

Steroidumwandelnde Enzyme aus Mikroorganismen IX. Affinitätschromatographische Präparation und Untersuchung des Apoenzyms einer 4‐En‐3‐oxosteroid: (Akzeptor)‐1‐en‐oxidoreduktase aus Nocardia opaca

Steroidumwandelnde Enzyme aus Mikroorganismen IX. Affinitätschromatographische Präparation und Untersuchung des Apoenzyms einer 4-En-3-oxosteroid: (Akzeptor)-1-en-oxidoreduktase ausNocardia opaca

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