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 Citation Map 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 HighWire Citing Articles via Google Scholar Google Scholar Articles by Braughler, J. M. Articles by Murad, F. Search for Related Content PubMed PubMed Citation Articles by Braughler, J. M. Articles by Murad, F. Social Bookmarking                      What's this?

JBC, Vol. 254, Issue 24, 12450-12454, Dec, 1979

Effects of thiols, sugars, and proteins on nitric oxide activation of guanylate cyclase

J. M. Braughler, C. K. Mittal and F. Murad

Purification of soluble guanylate cyclase from rat liver resulted in an apparent loss of enzyme activation by nitric oxide that could be restored by dithiothreitol. methemoglobin, bovine serum albumin, or sucrose. Although hemoglobin also permitted some activation with nitric oxide, the effect of other agents to restore enzyme activation was prevented with hemoglobin. As a result of enzyme purification, there is an alteration of the dose-response relationship for nitric oxide activation. After partial enzyme purification, relatively high concentrations of nitric oxide that were stimulatory in crude enzyme preparations had no effect on enzyme activity. However, partially purified or homogeneous enzyme was activated by lower concentrations of nitric oxide. The bell-shaped dose-response curve for nitric oxide was shifted to the left with guanylate cyclase purification. The addition of dithiothreitol, methemoglobin, bovine serum albumin, or sucrose to enzyme markedly broadens the dose-response curve for nitric oxide. Thus, the apparent loss of responsiveness to nitric oxide with purification is a function of increased sensitivity of guanylate cyclase to nitric oxide. Increased sensitivity to nitric oxide with enzyme purification probably results from the removal of heme, proteins, and small molecules that can serve as scavengers or sinks for nitric oxide and prevent excessive oxidation of the enzyme.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				L. Xu, C. Han, K. Lim, and T. Wu Activation of Cytosolic Phospholipase A2{alpha} through Nitric Oxide-induced S-Nitrosylation: INVOLVEMENT OF INDUCIBLE NITRIC-OXIDE SYNTHASE AND CYCLOOXYGENASE-2 J. Biol. Chem., February 8, 2008; 283(6): 3077 - 3087. [Abstract] [Full Text] [PDF]

				P. Pacher, J. S. Beckman, and L. Liaudet Nitric Oxide and Peroxynitrite in Health and Disease Physiol Rev, January 1, 2007; 87(1): 315 - 424. [Abstract] [Full Text] [PDF]

				B. Gomes, M. Savignac, M. D. Cabral, P. Paulet, M. Moreau, C. Leclerc, R. Feil, F. Hofmann, J.-C. Guery, G. Dietrich, et al. The cGMP/Protein Kinase G Pathway Contributes to Dihydropyridine-sensitive Calcium Response and Cytokine Production in TH2 Lymphocytes J. Biol. Chem., May 5, 2006; 281(18): 12421 - 12427. [Abstract] [Full Text] [PDF]

				S. F. Kim, D. A. Huri, and S. H. Snyder Inducible Nitric Oxide Synthase Binds, S-Nitrosylates, and Activates Cyclooxygenase-2 Science, December 23, 2005; 310(5756): 1966 - 1970. [Abstract] [Full Text] [PDF]

				Z. Dong, Y. Lavrovsky, M. A. Venkatachalam, and A. K. Roy Heme Oxygenase-1 in Tissue Pathology : The Yin and Yang Am. J. Pathol., May 1, 2000; 156(5): 1485 - 1488. [Full Text] [PDF]

				J. A. Melendez, R. P. Melathe, A. M. Rodriguez, J. E. Mazurkiewicz, and K. J. A. Davies Nitric Oxide Enhances the Manganese Superoxide Dismutase-dependent Suppression of Proliferation in HT-1080 Fibrosarcoma Cells Cell Growth Differ., September 1, 1999; 10(9): 655 - 664. [Abstract] [Full Text]

				A. A. Sadighi Akha, N. J. Willmott, K. Brickley, A. C. Dolphin, A. Galione, and S. V. Hunt Anti-Ig-induced Calcium Influx in Rat B Lymphocytes Mediated by cGMP through a Dihydropyridine-sensitive Channel J. Biol. Chem., March 29, 1996; 271(13): 7297 - 7300. [Abstract] [Full Text] [PDF]

				O. Zolle, A. M. Lawrie, and A. W. M. Simpson Activation of the Particulate and Not the Soluble Guanylate Cyclase Leads to the Inhibition of Ca2+ Extrusion through Localized Elevation of cGMP J. Biol. Chem., August 18, 2000; 275(34): 25892 - 25899. [Abstract] [Full Text] [PDF]