HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Auchus, R. J. Articles by Schaefer, J. Search for Related Content PubMed PubMed Citation Articles by Auchus, R. J. Articles by Schaefer, J. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 263, Issue 24, 11640-11645, Aug, 1988

Solid-state NMR observation of cysteine and lysine Michael adducts of inactivated estradiol dehydrogenase

RJ Auchus, DF Covey, V Bork and J Schaefer
Department of Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110.

The inactivation of estradiol dehydrogenase by enzyme-generated 3- hydroxy-14,15-secoestra-1,3,5(10)-trien-15-yn-17-one is accompanied by the formation of a lysine enaminone. The experiments leading to this conclusion involved degradation of the inactivated enzyme with Pronase and subsequent analysis by solution-state 13C NMR. The present paper reports solid-state 13C NMR experiments on lyophilized intact inactivated enzyme which are free from problems due to Pronase digestion. These experiments combine conventional cross-polarization and magic-angle spinning with selective irradiation of resonances arising from a 13C double label in the steroid. Magnetization transfer between neighboring 13C nuclei is used to simplify the spectra and to identify peaks due to label. The formation of cysteine and lysine Michael adducts of the enzyme is established by comparisons with chemical shifts of solid model adducts.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?