Characterization of bovine serum albumin glycated with glucose, galactose and lactose
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The non-enzymatic reaction between reducing sugars and proteins, known as glycation, has received increased attention from nutritional and medical research. In addition, there is a large interest in obtaining glycoconjugates of pure well-characterized oligosaccharides for biological research. In this study, glycation of bovine serum albumin (BSA) by d-glucose, d-galactose and d-lactose under dry-heat at 60°C for 30, 60, 120, 180 or 240 min was assessed and the glycated products studied in order to establish their biological recognition by lectins. BSA glycation was monitored using gel electrophoresis, determination of available amino groups and lectin binding assays. The BSA molecular mass increase and glycation sites were investigated by mass spectrometry and through digestion with trypsin and chymotrypsin. Depending on time and type of sugar, differences in BSA conjugation were achieved. Modified BSA revealed reduction of amino groups' availability and slower migration through SDS/PAGE. d-galactose was more reactive than d-glucose or d-lactose, leading to the coupling of 10, 3 and 1 sugar residues, respectively, after 120 minutes of reaction. BSA lysines (K) were the preferred modified amino acids; both K256 and K420 appeared the most available for conjugation. Only BSA-lactose showed biological recognition by specific lectins.
- Andon NL, Hollingworth S, Koller A, Greenland AJ, Yates JR III, Hanes PA (2002) Proteomic characterization of wheat amyloplasts using identification of proteins by tandem mass spectrometry. Proteomics 2: 1156-1168.
- Aring J, Schlepper-Schaefer J, Burkart V, Kolb H (1989) Nonenzymatically glycated serum albumin: interaction with galactose-specific liver lectins. Biochim Biophys Acta 1010: 140-144.
- Badui DS (1993) Química de los Alimentos. Tercera edición, pp 75. Pearson Educación. México DF.
- Berthold A, Schubert H, Brandes N, Kroh L, Miller R (2007) Behaviour of BSA and of BSA-derivatives at the air/water interface. Colloids Surf A Physicochem Eng Asp 301: 16-22.
- Boratyński J, Roy R (1998) High temperature conjugation of protein with carbohydrates. Glycoconj J 15: 131-138.
- Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding. Anal Biochem 72: 248-254.
- Chevalier F, Chobert JM, Genot C, Haertlé T (2001a) Scavenging of free radicals, antimicrobial, and cytotoxic activities of the Maillard reaction products of β-lactoglobulin glycated with several sugars. J Agric Food Chem 49: 5031-5038.
- Chevalier F, Chobert JM, Popineau Y, Nicolas MG, Haertlé T (2001b) Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar. Int Dairy J 11: 145-152.
- Chobert JM, Gaudin JC, Dalgalarrondo M, Haertlé T (2006) Impact of Maillard type glycation on properties of beta-lactoglobulin. Biotechnol Adv 24: 629-632.
- Ernst B, Oehrlein R (1999) Substrate and donor specificity of glycosyl transferases. Glycoconj J 16: 161-170.
- Fayle SE, Gerrard JA (2002) The Maillard Reaction, pp 1,2. Royal Society of Chemistry. Great Britain.
- Fayle SE, Healy JP, Brown PA, Reid EA, Gerrard JA, Ames JM (2001) Novel approaches to the analysis of the Maillard reaction of proteins. Electrophoresis 22: 1518-1525.
- Finot PA (2005) Historical perspective of the Maillard reaction in food science. Ann NY Acad Sci 1043: 1-8.
- Frister H, Meisel H, Schlimme E (1988) OPA method modified by use of N,N-dimethyl-2-mercaptoethylammonium chloride as thiol component. Frezenius Z Anal Chem 330: 631-633.
- Frolov A, Hoffmann P, Hoffmann R (2006) Fragmentation behavior of glycated peptides derived from d-glucose, d-fructose and d-ribose in tandem mass spectrometry. J Mass Spectrom 41: 1459-1469.
- Iberg N, Fluckiger R (1986) Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites. J Biol Chem 261: 13542-13545.
- Kanska U, Boratyński J (2002) Thermal glycation of protein by d-glucose and d-fructose. Arch Immunol Ther Exp (Warsz) 50: 61-66.
- Kato A, Minaki K, Kobayashi K (1993) Improvement of emulsifying properties of egg white proteins by the attachment of polysaccharide through Maillard reaction in a dry state. J Agric Food Chem 41: 540-543.
- Kato Y, Aoki T, Kato N, Nakamura R, Matsuda T (1995) Modification of ovalbumin with glucose 6-phosphate by amino-carbonyl reaction. Improvement of protein heat stability and emulsifying activity. J Agric Food Chem 43: 301-305.
- Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
- Lapolla A, Fenele D, Reitano R, Arico NC, Seraglia R, Traldi P, Marotta E, Tonani R (2004) Enzymatic digestion and mass spectrometry in the study of advanced glycation end products/peptides. J Am Soc Mass Spectrom 15: 496-509.
- Nacharaju P, Acharya S (1992) Amadori rearrangement potential of hemoglobin at its glycation sites is dependent on the three-dimensional structure of protein. Biochemistry 31: 12673-12679.
- Paschinger K, Fabini G, Schuster D, Rendić D, Wilson IB (2005) Definition of immunogenic carbohydrate epitopes. Acta Biochim Polon 52: 629-632.
- Sarabia-Sainz A, Vázquez-Moreno L, Ramos-Clamont G (2006) Biorecognition of E. coli K88 adhesin for glycated porcine albumin. Glycobiology 16: 1142.
- Scaloni A, Perillo V, Franco P, Fedele E, Froio R, Ferrara L, Bergamo P (2002) Characterization of heat-induced lactosylation products in caseins by immunoenzymatic and mass spectrometric methodologies. Biochim Biophys Acta 1598: 30-39.
- Shaklai N, Garlick RL, Bunn HF (1984) Nonenzymatic glycosylation of human serum albumin alters its conformation and function. J Biol Chem 259: 3812-3817.
- Sharon N (2006) Carbohydrates as future anti-adhesion drugs for infectious diseases. Biochim Biophys Acta 1760: 527-537.
- Shevchenko A, Wilm M, Vorm O, Mann M (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal Chem 68: 850-858.
- Stefanowicz P, Boratyński J, Kańska U, Petry I, Szewczuk Z (2001) Evaluation of high temperature glycation of proteins and peptides by electrospray ionization mass spectrometry. Acta Biochim Polon 48: 1137-1141.
- Stowell CP, Lee YC (1978) The binding of d-glucosyl-neoglycoproteins to the hepatic asialoglycoprotein receptor. J Biol Chem 253: 6107-6110.
- Tagami U, Akashi S, Mizukoshi T, Suzuki E, Hirayama K (2000) Structural studies of the Maillard reaction products of a protein using ion trap mass spectrometry. J Mass Spectrom 35: 131-138.
- Taylor ME, Drickamer K (2006) Introduction to Glycobiology. 2nd edn, pp 51. Oxford University Press, New York. .
- Varki A (1993) Biological roles of oligosaccharides: all the theories are correct. Glycobiology 3: 97-130.
- Varki A, Cummings R, Esko J, Freeze H, Hart G, Marth J (1999) Essentials of Glycobiology, pp 8. Cold Spring Harbor Laboratory Press, NY, USA.
- Wooster TJ, Augustin MA (2006) Beta-lactoglobulin-dextran Maillard conjugates: their effect on interfacial thickness and emulsion stability. J Colloid Interface Sci 303: 564-572.
- Yeboah FK, Yaylayan VA (2001) Analysis of glycated proteins by mass spectrometric techniques: qualitative and quantitative aspects. Nahrung/Food 45: 164-171
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