Mechanism of interaction of Pb(II) with milk proteins: A case study of α-casein

Journal of Agricultural and Food Chemistry

Volumn 55, Issue 22, 2007, Pages 9283-9288

  Srinivas, S ^a   Kaul, Purnima ^a   Prakash, V ^a  

^a CENTRAL FOOD TECHNOLOGICAL RESEARCH INSTITUTE   (India)

Author keywords

casein; Circular dichroism; Cysteines; Hydrophobicity; Lead; Milk; Raman spectra; Stopped flow

Indexed keywords

CASEIN; CYSTEINE; LEAD; MILK PROTEIN;

ARTICLE; BINDING SITE; CHEMISTRY; HYDROPHOBICITY; KINETICS; RAMAN SPECTROMETRY;

BINDING SITES; CASEINS; CYSTEINE; HYDROPHOBICITY; KINETICS; LEAD; MILK PROTEINS; SPECTRUM ANALYSIS, RAMAN;

BOVINAE;

EID: 36148977233     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf070911t     Document Type: Article

References (33)

1. Farrell, H. M., Jr.; Jimenez-Flores, R.; Bleck, G. T.; Brown, E. M.; Butler, J. E.; Creamer, L. K.; Hicks, C. L.; Hollar, C. M.; Ng-Kwai-Hang, K. F.; Swaisgood, H. E. Nomenclature of the proteins of cows' milk, sixth revision. J. Dairy Sci. 2004, 87, 1641-1674.
2. Matsudomi, N.; Kanda, Y.; Moriwaki, H. α-Casein improves the gel properties of dried egg white. J. Agric. Food Chem. 2003, 51, 7140-7145.
3. Mitra, G.; Saha, A.; Gupta, T. D.; Poddar, A.; Das, K. P.; Dasgupta, S. K.; Bhattacharyya, B. Chaperone-mediated inhibition of tubulin self-assembly. Proteins 2007, 67, 112-120.
4. Hira, T.; Hara, H.; Tomita, F.; Aoyama, Y. Casein binds to cell membrane and induces intracellular calcium signals in the entero endocrine cell: a brief communication. Exp. Biol. Med. (Maywood) 2003, 228, 850-854.
5. Syme, C. D.; Blanch, E. W.; Holt, C.; Jakes, R.; Goedert, M.; Hecht, L.; Barron, L. D. A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins. Eur. J. Biochem. 2002, 269, 148-156.
6. Smyth, E.; Syme, C. D.; Blanch, E. W.; Hecht, L.; Vasak, M.; Barron, D. L. Solution structure of native proteins with irregular folds from Raman optical activity. Biopolymers 2001, 58, 138-151.
7. Chanat, E.; Martin, P.; Ollivier-Bousquet, M. αS1 casein is required for the efficient transport of β and κ casein from the endoplasmic recticulum to the Golgi apparatus of mammary epithelial cells. J. Cell Sci. 1999, 112, 3399-3412.
8. Goering, P. L. Lead-protein interactions as a basis for lead toxicity. Neurotoxicology 1993, 14, 45-60.
9. Mailer, K.; Calhoun, L. A.; Livesey, D. L. Interaction of lead ions with carbonic anhydrase. Int. J. Pept. Protein Res. 1982, 18, 233-239.
10. Lonnerdal, B. Dietary factors effecting trace element bioavailability from human milk, cow's milk and infant formulas. Prog. Food Nutr. Sci. 1985, 9, 35-62.
11. Jeng, S. L.; Lee, S. J.; Lin, S. Y. Determination of cadmium and lead in raw milk by graphite furnace atomic absorption spectrophotometer. J. Dairy Sci. 1994, 77, 945-949.
12. Mannino, S.; Bianco, M. Studies on the complexation properties of casein with lead by Potentiometrie stripping analysis. Analyst 1988, 113, 87-89.
13. Skoog, D. A.; West, D. M.; Holler, F. J. Fundamentals of Analytical Chemistry, 7th ed.; Saunders Publishers: New York, 1995.
14. Hipp, N. J.; Groves, M. L.; Custer, J. H.; McMeekin, T. L. Separation of α-, β-, and γ-casein. J. Dairy Res. 1952, 35, 272-281.
15. Oberfelder, R. W.; Lee, J. C. Measurement of ligand protein interaction by electrophoretic and spectroscopic techniques. Methods Enzymol. 1985, 117, 381-399.
16. Scatchard, G. The attractions of proteins for small molecules and ions. Ann. N. Y. Acad. Sci. 1949, 51, 660-672.
17. Kato, A.; Nakai, S. Hydrophobicity determined by a fluorescent probe method and its correlation with surface hydrophobicity of proteins. Biochim. Biophys. Acta 1980, 624, 13-20.
18. s-casein with small ions. J. Am. Chem. Soc. 1965, 87, 110-117.
19. Waugh, D. F.; Ludwig, M. L.; Gillespie, J. M.; Melton, B.; Foley, M.; Kleiner, E. S. The aS-caseins of bovine milk. J. Am. Chem. Soc. 1962, 84, 4929-4938.
20. Yang, J. T.; Wu, C. S.; Martinez, H. M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 1986, 130, 208-269.
21. Xing, C. S.; Liang, H.; Guo, J. H.; Song, C.; He, W. X.; Yuan, Y. Z. J. Studies on the interaction between Ag(II) and human serum albumin. Inorg. Biochem. 2003, 95, 124130.
22. Oinuma, K. I.; Hideyuki, K.; Takehiro, O.; Konishi, K.; Hashimoto, Y.; Higashibata, H.; Kitagawa, T.; Shiro, Y.; Kobayashi, M. Stopped-flow spectrophotometric and resonance Raman analyses of aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis. FEBS Lett. 2005, 579, 1394-1398.
23. Gutfreund, H., Ed. In Enzymes: Physical Principles. Enzyme Kinetics: Steady State; Wiley: New York, 1972.
24. 2+ binding to α-lactalbumin. Biochem. Mol. Biol. Int. 1996, 39, 1255-1265.
25. Ayranci, E.; Duman, O. Binding of lead ion to bovine serum albumin studied by ion selective electrode. Protein Pept. Lett. 2004, 11, 331-337.
26. Kagi, J. H. R.; Hapke, H.-J. Biochemical interactions of mercury, cadmium and Pb(II). In Changing Metal Cycles and Human Cycles; Nriagu, J. O., Ed.; Springer-Verlag: New York, 1984; pp 237-550.
27. Godwin, H. A. The biological chemistry of lead. Curr. Opin. Chem. Biol. 2001, 5, 223-227.
28. 2+ binding to structural zinc-binding domains determined directly by monitoring lead-thiolate charge-transfer bands. J. Am. Chem. Soc. 1999, 121, 6850-6855.
29. Raso, S. W.; Clark, P. L.; Pettingell, H. C.; King, J.; Thomas, J. G., Jr. Distinct cysteine sulfhydryl environments detected by analysis of Raman S-H markers of Cys-Ser mutant proteins. J. Mol. Biol. 2001, 307, 899-911.
30. Te, A. J. In Raman Spectroscopy in Biology: Principles and Applications; Wiley: New York, 1952; pp 65-350.
31. Busenlehner, L. S.; Cosper, N. J.; Scott, R. A.; Rosen, B. P.; Wong, M. D.; Giedroc, D. P. Spectroscopic properties of the metalloregulatory Cd(II) and Pb (II) sites of S. aureus PI258 Cad C. Biochemistry 2001, 40, 4426-4436.
32. Rasmussen, L. K.; Hojrup, P.; Petersen, T. E. Localization of two interchain disulfide bridges in dimers of bovine α s2-casein. Parallel and antiparallel alignments of the polypeptide chains. Eur. J. Biochem. 1992, 203, 381-386.
33. Moreno, F.; Jimenez, G. Binding of the promen fluorescent probe to human serum albumin. Chem. Biol. Interact. 1999, 121, 237-252.