Cross-linking of proteins

Large multiprotein complexes often participate in ET reactions but are also responsible for many other biological processes. Currently, the design of photoactive reagent, which would cross-link the associated proteins, seems to be a promising method for probing the dynamics of protein-protein interactions [107-111], The 

---

The transglutaminases are calcium-dependent enzymes that catalyse the cross-linking of proteins by promoting the formation of isopeptide bonds between the /-carboxyl group of a glutamine in one polypeptide chain and the e-amino group of a lysine in the second (Greenberg et al., 1991). These... 

In either dilute or concentrated solutions, additional reactions occur that result in both intra- and intermolecular cross-linking of proteins. There is little direct chemical information from such techniques as nuclear magnetic resonance spectroscopy or mass spectrometry to detail the precise nature of these cross-links.5,6... 

Avrameas, S., and Ternynck, T. (1969) The cross-linking of proteins with glutaraldehyde and its use for the preparation of immunosorbents. Immunochemistry 6, 53-66. 

Gorman, J.J., and Folk, J.E. (1980) Transglutaminase amine substrates for photochemical labeling and cleavable cross-linking of proteins./. Biol. Chem. 255, 1175. 

Hardy, P.M., Nicholls, A.C., and Rydon, H.N. (1976) The nature of the cross-linking of proteins by glutaraldehyde. Interaction of glutaraldehyde with the amino-groups of 6-ami-nohexanoic acid and of b-N-acetyl-lysine. J. Chem. Soc., Perk Trans. 1, 958. 

Mikkelsen, R.B., and Wallach, D.F.H. (1976) Photoactivated cross-linking of protein within the erythrocyte membrane core./. Biol. Chem. 251, 7413. 

Partis, M.D., Griffiths, D.G., Roberts, G.C., and Beechey, R.B. (1983) Cross-linking of protein by w-maleimido alkanoyl N-hydroxysuccinimido esters./. Protein Chem. 2, 263-277. 

Traut, R.R., Casiano, C., and Zecherle, N. (1989) Cross-linking of protein subunits and ligands by the introduction of disulfide bonds. In Protein Function—A Practical Approach (T.E. Creighton, ed.), pp. 101-133. IRL Press at Oxford University, Oxford. 

Fig. 12. Cross-linking of proteins within the E. coli (a) 30 S and (b) 50 S subunits (Traut et at., 1980). Asterisks denote proteins cross-linked to initiation factors, (c) Protein neig h-borhoods at the subunit interface (Lambert and Traut, 1981). Scheme 1 shows the crosslinks found in highest amount Scheme 2 those among 50 S proteins LI and L2 and several 30 S proteins and Scheme 3 those between 5 S RNA binding proteins and 30 S proteins. Reproduced with permission from Wittmann (1983).

Heinecke, J.W., Tyrosyl radical production by myeloperoxidase a phagocyte pathway for lipid peroxidation and dityrosine cross-linking of proteins, Toxicology, 177, 11, 2002. 

The attachment of sugars to the protein increases its hydrophilicity however, solubility may be reduced, probably due to cross-linking of protein molecules. 

Cross-linking of proteins. Covalent cross-linking of caseins is evident (by gel electrophoresis) after even 2 min at 140°C and it is not possible to resolve the heat-coagulated caseins by urea- or SDS-PAGE. 

We dry chow ski A, Schmidt WN, Hnilica LS. 1986. The in-vivo cross-linking of proteins and DNA by heavy metals. J Biol Chem 261 3370. 

PM Hardy, AC Nicholls, HN Rydon. Nature of cross-linking of proteins by glutaral-dehyde. 1. Interaction of glutaraldehyde with amino groups of 6-aminohexanoic acid and of a-N-acetyl-L-lysine. J Chem Soc, Perkin Trans I 958-962, 1976. 

M. O. Lederer and R. G. Klaiber, Cross-linking of proteins by Maillard processes Characterization and detection of lysine-arginine cross-links derived from glyoxal and methylglyoxal, Bioorg. Med. Chem., 1999, 7, 2499-2507. 

F. Gerum, M. O. Lederer, and T. Severin, Cross-linking of proteins by Maillard processes Model reaction of an Amadori compound with W -acctyl-l -arginine, in F. 1998, 409. 

Kortenkamp A, Curran B, O Brien P. 1992. Defining conditions for the efficient in vitro cross-linking of proteins to DNA by chromium(III) compounds. Carcinogenesis 13(2) 307-308. 

Fancy DA, Denison C, Kim K, et al. Scope, limitations and mechanistic aspects of the photo-induced cross-linking of proteins by water-soluble metal complexes. Chem Biol 2000 7 697-708. 

Peroxidases oxidize tyrosines, both as a free amino acid and as a residue in peptides and proteins. When proteins are treated with HRP in the presence of hydrogen peroxide, protein dimers are obtained through the coupling of tyrosyl radicals. HRP can also be used for cross-linking of proteins with polysaccharides [35]. In this case, coupling occurs between a tyrosyl radical in the protein and a radical species on the saccharide ... 

Matheis G, Whitaker JR (1984) Peroxidase-catalyzed cross linking of proteins. J Prot Chem 3 35-48... 

Matheis G, Whitaker JR (1987) A review enzymatic cross-linking of proteins appilcable to foods. J Food Biochem 11 309-327... 

---