Study of the effect of Cal-Red on the secondary structure of human serum albumin by spectroscopic techniques

Journal of Molecular Structure

Volumn 846, Issue 1-3, 2007, Pages 112-118

  Dong, Lijun ^a   Chen, Xingguo ^a   Hu, Zhide ^a  

^a LANZHOU UNIVERSITY   (China)

Author keywords

Cal Red; Circular dichroism (CD); Fourier transformed IR; Human serum albumin; Resonance light scattering; Thermodynamics

Indexed keywords

DICHROISM; FOURIER TRANSFORM INFRARED SPECTROSCOPY; LIGHT SCATTERING; RESONANCE; THERMODYNAMIC PROPERTIES;

FOURIER TRANSFORMED IR; HUMAN SERUM ALBUMIN; RESONANCE LIGHT SCATTERING;

PROTEINS;

EID: 35548972918     PISSN: 00222860     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molstruc.2007.01.034     Document Type: Article

References (33)

1. Peters T. Adv. Protein Chem. 37 (1985) 161-242
2. Curry S., Brick P., and Franks N.P. Biochem. Biophys. Acta 1441 (1999) 131-140
3. Peters T. Biochemistry, Genetics and Medical Applications (1996), Academic Press, San Diego, CA
4. Cater D.C., and Ho J.X. Adv. Protein Chem. 45 (1994) 153-203
5. He H.M., and Cater D.C. Nature 358 (1992) 209-215
6. Petitpas I., Crune T., Battacharya A.A., and Curry S.J. Mol. Biol. 314 (2001) 955-960
7. Trynda-Lemiesz L., Karacyzn A., Keppler B.K., and Kozlowski H. J. Inorg. Biochem. 78 (2000) 341-346
8. Pelton J.T., and Mclean L.R. Anal. Biochem. 277 (2000) 167-176
9. Jiang M., Xie M.X., Zheng D., Liu Y., Li X.Y., and Chen X. J. Mol. Struct. 692 (2004) 71-80
10. Trynda-Lemiesz L. Bioorg. Med. Chem. 12 (2004) 3269-3275
11. Gao H., Lei L.D., Liu J.Q., Kong Q., Chen X.G., and Hu Z.D. J. Photochem. Photobiol. A 167 (2004) 213-221
12. He W.Y., Li Y., Tian J.N., Liu H.X., Hu Z.D., and Chen X.G. J. Photochem. Photobiol. A 174 (2005) 53-61
13. Li Y., He W.Y., Liu J.Q., Sheng F.L., Hu Z.D., and Chen X.G. BBA-Gen. Subject 1722 (2005) 15-21
14. Dong L.J., He J., Li Q.F., Chen X.G., and Hu Z.D. Anal. Biochem. 315 (2003) 22-28
15. Hong H.Y., Choi J.K., and Yoo G.S. Anal. Biochem. 214 (1993) 96-99
16. Jung D.W., Yoo G.S., and Choi J.K. electrophoresis 19 (1998) 2412-2415
17. Kirschembaum D.M. Handbook of Biochemistry, Selected Data for Molecular Biology. second ed. (1970), Chemical Rubber Company, Cleveland, OH
18. Dong A.C., Huang P., and Caughey W.S. Biochemistry 29 (1990) 3303-3308
19. Greenfield N., and Fasman G.D. Biochemistry 8 (1969) 4108-4116
20. Anglister J., and Steinberg I.Z. Chem. Phys. Lett. 65 (1979) 50-54
21. Strothkamp K.G., and Strothkamp R.E. J. Chem. Educ. 71 (1994) 77-79
22. Scatchard G., Scheinberg I.H., and Armstrong S.H. J. Am. Chem. Soc. 72 (1950) 535-540
23. Wi S., Pancoska P., and Keiderling T.A. Biospectroscopy 4 (1998) 93-99
24. Rahmelow K., and Hubner W. Anal. Biochem. 241 (1996) 5-11
25. Singh B.R., Fuller M.P., and Schiavo G. Biophys. Chem. 36 (1990) 155-161
26. Neault J.F., Novetta-delen A., Arakawa H., Malonga H., and Tajmir-Riahi H.A. Can. J. Chem. 78 (2000) 291-296
27. Gaudreau S., Neault J.F., and Tajmir-Riahi H.A. J. Biomol. Struct. Dyn. 19 (2002) 1007-1014
28. Ouameur A.A., Mangier E., Diamantoglou S., Rouillon R., Carpentier R., and Tajmir-Riahi H.A. Biopolymers 73 (2004) 503-509
29. Ouameur A.A., Marty R., and Tajmir-Riahi H.A. Biopolymers 77 (2005) 129-136
30. Ragi C., Sedaghat-Herati M.R., Ouameur A.A., and Tajmir-Riahi H.A. Biopolymers 78 (2005) 231-236
31. Juziro N., and Noriko M. Chem. Pharm. Bull. 33 (1985) 2522-2524
32. Rahman M.H., Yamasaki K., Shin Y.H., Lin C.C., and Otagiri M. Biol. Pharm. Bull. 16 (1993) 1169-1174
33. Ross P.D., and Subramanian S. Biochemistry 20 (1981) 3096-3102