If κ is measurable, Prikry's forcing adds a sequence of ordinals of order type ω cofinal in κ. This destroys the regularity of κ but κ does remain uncountable. Magidor has a forcing notion generalizing Prikry's which adds a closed cofinal sequence of ordinals through a large cardinal. The cardinal remains uncountable but uts regularity is still destroyed. We obtain a forcing notion which adds a closed cofinal sequence of ordinals (and more complex objects) through a large cardinal κ, of order type κ, and keeps κ regular. In fact κ remains measurable after the forcing.

FEBS LettersVolume 80, Issue 1 p. 1-4 Full-length articleFree Access Subunit structure and physical properties of an NADP (H) -binding protein from human erythrocytes A. Morelli, A. Morelli Institute of Biochemistry, University of Genoa, Viale Benedetto XV-1, 16132 Genoa, ItalySearch for more papers by this authorU. Benatti, U. Benatti Institute of Biochemistry, University of Genoa, Viale Benedetto XV-1, 16132 Genoa, ItalySearch for more papers by this authorL. Radin, L. Radin Institute of Microbiology, University of Genoa, Viale Benedetto XV-1, 16132 Genoa, ItalySearch for more papers by this authorN.G. Wrigley, N.G. Wrigley National Institute for Medical Research, Mill Hill, London NW 7 1AA, EnglandSearch for more papers by this authorA. De Flora, A. De Flora Institute of Biochemistry, University of Genoa, Viale Benedetto XV-1, 16132 Genoa, ItalySearch for more papers by this author A. Morelli, A. Morelli Institute of Biochemistry, University of Genoa, Viale Benedetto XV-1, 16132 Genoa, ItalySearch for more papers by this authorU. Benatti, U. Benatti Institute of Biochemistry, University of Genoa, Viale Benedetto XV-1, 16132 Genoa, ItalySearch for more papers by this authorL. Radin, L. Radin Institute of Microbiology, University of Genoa, Viale Benedetto XV-1, 16132 Genoa, ItalySearch for more papers by this authorN.G. Wrigley, N.G. Wrigley National Institute for Medical Research, Mill Hill, London NW 7 1AA, EnglandSearch for more papers by this authorA. De Flora, A. De Flora Institute of Biochemistry, University of Genoa, Viale Benedetto XV-1, 16132 Genoa, ItalySearch for more papers by this author First published: August 01, 1977 https://doi.org/10.1016/0014-5793(77)80393-1Citations: 9AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume80, Issue1August 01, 1977Pages 1-4 ReferencesRelatedInformation

A number of derivatives of NADP(H) were tested with respect to their effectiveness in interacting with tetrameric glucose 6-phosphate dehydrogenase (G6PD) retaining only the fraction of "structural" coenzyme (4 moles NADP). Interaction was probed by two parameters: a) increased thermostability of G6PD activity, measured as the difference in the corresponding transition temperature (Tm) of samples containing and lacking the NADP derivatives, respectively; b) competitive inhibition toward NADP, expressed a Ki values. Protection afforded by the various effectors against thermal denaturation decreased in the following order: NADPH, NADP, PADP-ribose, adenosine 2',5'-P2. Other NADP derivatives, including 2',3' cyclic NADP, NMN, NMNH, nicotinamide, adenosine 2'-P, were uneffective in respect to this property. The kinetically measured affinity was the greatest for NADPH and decreased progressively for the following effectors: PADP-ribose, NADP, NMNH, PADP-glycolaldehyde, adenosine 2',5'-P2, PADP-ribitol, adenosine 2'-P. Nicotinamide and NMN were uneffective on NADP binding. These data show that the adenosine moiety of NADP is more critically involved than the nicotinamide portion in the interaction with human G6PD.