The secondary structure of human Hageman factor (factor XII) and its alteration by activating agents

The Journal of Clinical Investigation
C R McMillinA G Walton

Abstract

Hageman factor (factor XII) is activated by exposure to surfaces such as glass or by solutions of certain compounds, notably ellagic acid. Changes in the structure of Hageman factor accompanying activation have been examined in this study by circular dichroism spectroscopy. The spectrum of unactivated Hageman factor in aqueous solutions suggests that its conformation is mainly aperiodic. Various perturbants altered the conformation of Hageman factor in differing ways, demonstrating the sensitivity of Hageman factor to its environment. After activation of Hageman factor with solutions of ellagic acid, a negative trough appeared in the region of the circular dichroism spectrum commonly assigned to tyrosine residues, along with other minor changes in the peptide spectral region. Some of these changes are similar to changes that occurred upon partial neutralization of the basic residues at alkali pH. Activation of Hageman factor by adsorption to quartz surfaces (in an aqueous environment) also produced changes similar to those in the ellagic acid-activated Hageman factor, including the negative ellipticity in the tyrosine region. These observations suggest that the activation process may be related to a change in status of some of ...Continue Reading

References

Mar 1, 1988·Somatic Cell and Molecular Genetics·N J RoyleJ L Hamerton
Feb 2, 1999·Clinical Reviews in Allergy & Immunology·A P KaplanM Silverberg
Feb 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·O D Ratnoff, H Saito
Mar 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·O D Ratnoff, H Saito
Nov 1, 1979·The Journal of Experimental Medicine·R C Wiggins, C G Cochrane
Sep 16, 1985·European Journal of Biochemistry·J RosingJ H Griffin
Jul 15, 1997·European Journal of Biochemistry·R Røjkaer, I Schousboe
Nov 1, 1986·Biological Reviews of the Cambridge Philosophical Society·C A Finn
Sep 1, 1983·The Journal of Clinical Investigation·H SaitoA Angell
Jul 1, 1986·The Journal of Clinical Investigation·E J GustafsonA Schmaier
Nov 15, 1980·Thrombosis Research·M F ScullyV V Kakkar
Jul 8, 1980·Biochemistry·D L TankersleyD D Schroeder
Apr 1, 1980·Biochemistry·K FujikawaE W Davie
Jan 17, 1984·Biochemistry·D L Tankersley, J S Finlayson
Aug 1, 1987·Archives of Biochemistry and Biophysics·R A PixleyR W Colman
Jan 1, 1982·Annals of the New York Academy of Sciences·A P KaplanB Ghebrehiwet
Jan 1, 1987·Annals of the New York Academy of Sciences·M Silverberg, S V Diehl
Jan 1, 1981·Annals of the New York Academy of Sciences·P N Walsh, J H Griffin
Jan 1, 1980·CRC Critical Reviews in Biochemistry·Y Nemerson, B Furie
Apr 1, 1988·Journal of Biomedical Materials Research·C R McMillinS P Schmidt

Citations

Apr 1, 1973·The Journal of Clinical Investigation·H SaitoJ Pensky
Dec 1, 1973·The Journal of Experimental Medicine·C G CochraneK D Wuepper
May 3, 1969·Nature·W B Gratzer, D A Cowburn
Jan 1, 1972·Biopolymers·V Madison, J Schellman
Jun 20, 1972·Biochemistry·C A Bush, D E Gibbs
Jan 1, 1971·Biopolymers·W B Rippon, A G Walton
May 1, 1966·Proceedings of the National Academy of Sciences of the United States of America·E Iizuka, J T Yang
May 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·V P Saxena, D B Wetlaufer
Sep 15, 1970·The Journal of Chemical Physics·D Aebersold, E S Pysh
Apr 13, 1971·Biochemistry·S M Ziegler, C A Bush
May 22, 1968·Journal of the American Chemical Society·F Quadrifoglio, D W Urry
Jan 1, 1968·Biopolymers·M L Tiffany, S Krimm
Oct 1, 1968·Biochemistry·L StevensJ Potter
Mar 1, 1969·Journal of Biomedical Materials Research·J L Brash, D J Lyman
May 1, 1969·Biochemistry·I ListowskyG Avigad
Nov 5, 1965·Science·V H Donaldson, O D Ratnoff
Jul 1, 1965·Biochimica Et Biophysica Acta·J G SchoenmakersF Zilliken
Sep 13, 1967·Journal of the American Chemical Society·N S Simmons, A N Glazer
Nov 1, 1962·Biochemistry·O D Ratnoff, E W Davie

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