Investigation of guanidine hydrochloride induced unfolding of apolipoprotein A-IMilano

Spectroscopy

Volumn 16, Issue 3-4, 2002, Pages 199-206

  Suurkuusk, Malin ^a,b   Hallén, Dan ^a  

^a BIOVITRUM AB   (Sweden)

^b Thermometric AB   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETRY; CENTRIFUGATION; HYDROCHLORIC ACID; LIPIDS; PROTEINS; SEDIMENTATION; SODIUM COMPOUNDS; TITRATION;

CIRCULAR DICHROISM (CD) MEASUREMENTS;

SPECTROSCOPIC ANALYSIS;

APOLIPOPROTEIN A1; GUANIDINE; SODIUM DIHYDROGEN PHOSPHATE;

ALPHA HELIX; ARTICLE; CALORIMETRY; CIRCULAR DICHROISM; CONTROLLED STUDY; DISSOCIATION; ENTHALPY; NONHUMAN; PROTEIN AGGREGATION; PROTEIN STRUCTURE; SEDIMENTATION; VELOCITY;

EID: 0036965555     PISSN: 07124813     EISSN: None     Source Type: Journal    
DOI: 10.1155/2002/201073     Document Type: Article

References (19)

1. J.A. Glomset, The plasma lecithin: Cholesterol acyltransferase reaction, J. Lip. Res. 9 (1968), 155-162.
2. Q.-H. Meng, L. Calabresi, J.-C. Fruchart and Y.L. Marcel, Apolipoprotein AI domains involved in the activation of lecithin: cholesterol acyltransferase, J. Biol. Chem. 268 (1993), 16 966-16 973.
3. A.R. Tall, Plasma high density lipoproteins, J. Clin. Invest. 86 (1990), 379-384.
4. H.B. Brewer Jr., T. Fairwell, A. LaRue, R. Ronan, A. Houser and T.J. Bronzert, The amino acid sequence of human apoA-I, an apolipoprotein isolated from high density lipoproteins, Biochem. Biophys. Res. Com. 80 (1978), 623-630.
5. J.P. Segrest, M.K. Jones, H. Deloof, C.G. Brouillette, Y.V. Venkatachalapathi and G.M. Anantharamaiah, The amphiphathic helix in the exchangeable apolipoproteins - A review of secondary structure and function, J. Lip. Res. 33 (1992), 141-166.
6. D.L. Barbeau, A. Jonas, T.-I. Teng and A.M. Scanu, Asymmetry of apolipoprotein A-I in solution assessed from ultracentrifugal, viscometric, and fluorescence polarization studies, Biochemistry 18 (1979), 362-369.
7. Milano dimer, J. Biol. Chem. 269 (1994), 32 168-32 174.
8. G. Franceschini, P. Apebe, L. Calabresi, V. Gualandri and C.R. Sirtori, Apolipoprotein A-I, Milano variant: Genetic, clinical and biochemical features, Aterosclerosis Rev. 16 (1987), 149-159.
9. S.C.R. Weisgraber Jr., T.P. Bersot, R.W. Mahley, G. Franceschini and C.R. Sirtori, Apolipoprotein A-IMilano, J. Biol. Chem. 258 (1983), 2508-2513.
10. L. Calabresi, G. Vecchio, F. Frigerio, L. Vavassori, C.R. Sirtori and G. Franceschini, Reconstituted high-density lipoproteins with a disulfide-linked apolipoprotein A-I dimer: Evidence for restricted particle size heterogeneity, Biochemistry 36 (1997), 12 428-12 433.
11. M. Suurkuusk and S.K. Singh, Formation of HDL-like complexes from apolipoprotein A-I-M and DMPC, Int. J. Pharm. 194 (2000), 21-38.
12. M. Suurkuusk and D. Hallén, Apolipoprotein A-IMilano unfolds via an intermediate state as studied by differential scanning calorimetry and circular dichroism, Eur. J. Biochem. 264 (1999), 183-190.
13. M. Suurkuusk and D. Hallén, Denaturation of apolipoprotein A-I and the monomer form of apolipoprotein, Eur. J. Biochem. 265 (1999), 346-352.
14. W. Pfeil and P.L. Privalov, Thermodynamic investigations of proteins. II. Calorimetric study of lysozyme denaturation by guanidine hydrochloride, Biophys. Chem. 4 (1976), 33-40.
15. G.I. Makhatadze and P.L. Privalov, Protein interactions with urea and guanidinium chloride: A calorimetric study, J. Mol. Biol. 226 (1992), 491-505.
16. P. Schuck, Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling, Biophys. J. 78 (2000), 1606-1619.
17. B.-M. Backlund, G. Wikander, T.L. Peeters and A. Gräslund, Induction of secondary structure in the peptide hormone motilin by interaction with phospholipid vesicles, Biochem. Biophys. Acta 1190 (1994), 337-344.
18. C. Tanford, Theoretical models for the mechanism of denaturation, Adv. Prot. Chem. 24 (1970), 1-95.
19. C. Edelstein and A.M. Scanu, Effect of guanidine hydrochloride on the hydrodynamic and thermodynamic properties of human apolipoprotein A-I in solution, J. Biol. Chem. 255 (1980), 5747-5754.