[71] Steroid-Transforming Enzymes

Ann M. Benson, Anthony J. Suruda, Evelyn R. Barrack, Paul Talalay

Research output: Contribution to journalArticle

Abstract

Affinity chromatography on adsorbents containing steroidal substrate analogs covalently linked to agarose promises to be an extremely valuable technique both for the purification of steroid-transforming enzymes, and for studies on their mechanism. When Pseudomonas testosteroni is grown on media containing certain steroids, crude extracts of lyophilized or sonically disrupted cells are a rich source of various induced steroid transforming enzymes. The isolation from these mixtures of discrete catalytic proteins, in purified form and uncontaminated by each other, has been a challenging task. The availability of such purified enzymes would greatly augment their suitability for the microanalysis and determination of steric configuration of steroids. Affinity techniques have indicated that the fl-enzymes do not bind strongly to steroids in the absence of NAD+, thus suggesting that these oxidations may involve an obligatory ordered addition in which the binding of NAD+ precedes that of the steroidal substrate.

Original languageEnglish (US)
Pages (from-to)557-566
Number of pages10
JournalMethods in enzymology
Volume34
Issue numberC
DOIs
StatePublished - Jan 1 1974

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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    Benson, A. M., Suruda, A. J., Barrack, E. R., & Talalay, P. (1974). [71] Steroid-Transforming Enzymes. Methods in enzymology, 34(C), 557-566. https://doi.org/10.1016/S0076-6879(74)34074-8