1-anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation

Biophysical Journal

Volumn 74, Issue 1, 1998, Pages 422-429

  Matulis, Daumantas ^a,b   Lovrien, Rex ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

^b VILNIUS UNIVERSITY   (Lithuania)

Author keywords

[No Author keywords available]

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ANION; BOVINE SERUM ALBUMIN; LYSOZYME; PAPAIN; POLYAMINOACID; POLYARGININE; POLYHISTIDINE; POLYLYSINE; PROTEIN; PROTEINASE; PROTON;

ARTICLE; CALORIMETRY; ENTHALPY; PH; PROTEIN BINDING; STOICHIOMETRY;

EID: 0031972919     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77799-9     Document Type: Article

References (16)

1. Cardamone, M., and N. Puri. 1992. Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochem. J. 282:589-593.
2. Carter, D., and J. Ho. 1994. Structure of serum albumin. Adv. Protein Chem. 45:153-203.
3. Conroy, M., and R. Lovrien. 1992. Matrix coprecipitating and cocrystallizing ligands (MCC ligands) for bioseparations. J. Cryst. Growth. 122:213-222.
4. Daniel, E., and G. Weber. 1966. Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalenesulfonate. Fluorimetric titrations. Biochemistry. 5:1893-1900.
5. Dubois, T., A. Jacquet, A. Schnek, and Y. Looze. 1988. Biol. Chem. Hoppe Seyler. 369:733-740.
6. Kane, C., and D. Bernlohr. 1996. A simple assay for intracellular lipid-binding proteins using displacement of 1-anilinonaphthalene 8-sulfonic acid. Anal. Biochem. 233:197-204.
7. Kirk, W., E. Kurian, and F. Prendergast. 1996. Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-(1′)anilinonaphthalene binding to intestinal fatty acid binding protein. Biophys. J. 70:69-83.
8. Matulis, D., T. Richardson, and R. Lovrien. 1996. Coprecipitation of proteins with matrix ligands: scaleable protein isolation. J. Mol. Recognit. 9:433-443.
9. Ojala, W., E. Sudbeck, L. Lu, T. Richardson, R. Lovrien, and W. Gleason. 1996. Complexes of lysine, histidine, and arginine with sulfonated azo dyes: model systems for understanding the biomolecular recognition of glycosaminoglycans by proteins. J. Am. Chem. Soc. 118:2131-2142.
10. Russell, V. A., M. C. Etter, and M. D. Ward. 1994. Layered materials by molecular design: structural enforcement by hydrogen bonding in guanidinium alkane-and arenesulfonates. J. Am. Chem. Soc. 116: 1941-1952.
11. Semisotnov, G., N. Rodionova, O. Razgulyaev, V. Uversky, A. Gripaś, and R. Gilmanshin. 1991. Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers. 31: 119-128.
12. Silverstein, R., and F. Kezdy. 1975. Characterization of pineapple stem proteases (bromelains). Arch. Biochem. Biophys. 167:678-686.
13. Slavik, J. 1982. Anilinonaphthalene sulfonate as a probe of membrane composition and function. Biochim. Biophys. Acta. 694:1-25.
14. Stryer, L. 1965. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe for nonpolar sites. J. Mol. Biol. 13:482-495.
15. Tanford, C., J. Buzzell, D. Rands, and S. Swanson. 1955a. The reversible expansion of bovine serum albumin in acid solutions. J. Am. Chem. Soc. 77:6421-6428.
16. Tanford, C., S. Swanson, and W. Shore. 1955b. Hydrogen ion equilibria of bovine serum albumin. J. Am. Chem. Soc. 77:6414-6421.