Determination of protein oligomerization state: Two approaches based on glutaraldehyde crosslinking

Analytical Biochemistry

Volumn 373, Issue 2, 2008, Pages 404-406

  Fadouloglou, Vasiliki E ^a,b   Kokkinidis, Michael ^a,c   Glykos, Nicholas M ^b  

^a UNIVERSITY OF CRETE   (Greece)

^b DEMOCRITUS UNIVERSITY OF THRACE   (Greece)

^c INSTITUTE OF MOLECULAR BIOLOGY AND BIOTECHNOLOGY   (Greece)

Author keywords

[No Author keywords available]

Indexed keywords

OLIGOMERS; PROTEINS; REAGENTS;

AMINO GROUP; BIOPHYSICAL METHODS; DETERMINATION OF PROTEINS; GLUTARALDEHYDE CROSS-LINKING; GLUTARALDEHYDES; REACTION CONDITIONS; RELIABLE RESULTS;

OLIGOMERIZATION;

GLUTARALDEHYDE; PROTEIN;

ARTICLE; CROSS LINKING; EXPERIMENTAL STUDY; OLIGOMERIZATION; PRIORITY JOURNAL;

EID: 37649022489     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.10.027     Document Type: Article

References (15)

1. Simanshu D.K., Savithri H.S., and Murthy M.R.N. Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation. J. Biol. Chem. 281 (2006) 39630-39641
2. Fang Y., Kolmakova-Partensky L., and Miller C. A bacterial arginine-agmatine exchange transporter involved in extreme acid resistance. J. Biol. Chem. 282 (2007) 176-182
3. Onica D., Mota G., Calugaru A., Manciulea M., and Dima S. Immunogenicity and effector functions of glutaraldehyde-treated rabbit and mouse immunoglobulin. G. Mol. Immunol. 20 (1983) 709-718
4. 2+ -ATPase of sarcoplasmic reticulum. Biochemistry 24 (1985) 1244-1251
5. Kapoor M., and O'Brien M.D. Investigation of the quaternary structure of Neurospora pyruvate kinase by cross-linking with bifunctional reagents: the effect of substrates and allosteric ligands. Can. J. Biochem. 55 (1977) 43-49
6. Kiernan J.A. Formaldehyde, formalin, paraformaldehyde and glutaraldehyde: what they are and what they do. Microscopy Today 00-1 (2000) 8-12
7. Lundblad R.L., and Noyes C.M. Chemical Reagents for Protein Modification (1984), CRC Press, Boca Raton, FL 123-139
8. Payne J.W. Polymerization of proteins with glutaraldehyde. Biochem. J. 135 (1973) 867-873
9. Pillai S., and Bachhawat B.K. Affinity immobilization and "negative" crosslinking: a probe for tertiary and quaternary protein structure. J. Mol. Biol. 131 (1979) 877-881
10. Lusty C.J. A gentle vapor-diffusion technique for cross-linking of protein crystals for cryocrystallography. J. Appl. Crystallogr. 32 (1999) 106-112
11. Janknedht R., Martynoff G., Lou J., Hipskind R., Nordheim A., and Stunnenberg H.G. Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus. Proc. Natl. Acad. Sci. USA 88 (1991) 8972-8976
12. Pillai S., and Bachhawat B.K. Protein-protein conjugation on a lectin matrix. Biochem. Biophys. Res. Commun. 75 (1977) 240-245
13. Banner D.W., Kokkinidis M., and Tsernoglou D. Structure of the ColE1 rop protein at 1.7 Å resolution. J. Mol. Biol. 196 (1987) 657-675
14. Fadouloglou V.E., Deli A., Glykos N.M., Psylinakis E., Bouriotis V., and Kokkinidis M. Crystal structure of the BcZBP, a zinc-binding protein from Bacillus cereus: functional insights from structural data. FEBS J. 274 (2007) 3044-3054
15. Fadouloglou V.E., Kotsifaki D., Gazi A.D., Fellas G., Meramveliotaki C., Deli A., Psylinakis E., Bouriotis V., and Kokkinidis M. Purification, crystallization and preliminary characterization of a putative LmbE-like deacetylase from Bacillus cereus. Acta Crystallogr. F 62 (2006) 261-264