Monosaccharide composition and properties of a deglycosylated turnip peroxidase isozyme

Phytochemistry

Volumn 62, Issue 1, 2003, Pages 5-11

  Duarte Vázquez, Miguel A ^a   García Almendárez, Blanca E ^a   Rojo Domínguez, Arturo ^b   Whitaker, John R ^c   Arroyave Hernandez C ^a   Regalado, Carlos ^a  

^a UNIVERSIDAD AUTÓNOMA DE QUERÉTARO   (Mexico)

^b DEPARTAMENTO DE QUÍMICA   (Mexico)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Brassica napus L. var. purple top white globe; Chemical deglycosylation; Cruciferae; Enzymatic deglycosylation; Turnip peroxidase

Indexed keywords

ACETYLNEURAMINYL HYDROLASE; BETA GALACTOSIDASE; BETA GALACTOSIDASE III; CARBOHYDRATE; FUCOSE; GLYCOPROTEIN; HEXASE I; HYDROGEN PEROXIDE; HYDROLASE; ISOENZYME; MANNOSE; MONOSACCHARIDE; N GLYCOSIDASE F; OLIGOSACCHARIDE; PERIODATE; PEROXIDASE; POLYCLONAL ANTIBODY; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; DEGLYCOSYLATION; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME PURIFICATION; MOLECULAR STABILITY; PROTEIN CONFORMATION; PROTEIN DEGRADATION; THERMOSTABILITY; TURNIP;

BRASSICA NAPUS; ENZYME STABILITY; GLYCOSYLATION; HEAT; HYDROGEN PEROXIDE; ISOENZYMES; KINETICS; OXIDATION-REDUCTION; PEROXIDASE; PROTEIN STRUCTURE, SECONDARY; TRYPSIN;

BRASSICA; BRASSICA NAPUS; BRASSICA RAPA SUBSP. RAPA; BRASSICACEAE; HYPTIS PECTINATA; ORYCTOLAGUS CUNICULUS;

EID: 0038601418     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0031-9422(02)00456-9     Document Type: Article

References (44)

1. Aluko, R.E., Yada, R.Y., Lencki, R.W., Marangoni, A., 1997. Structural and functional properties of partially purified cowpea (Vigna unguiculata) globulin modified with protein kinase and glycopeptidase. Journal of Agricultural and Food Chemistry 45, 2907-2913.
2. Andrade, M.A., Chacón, P., Merelo, J.J., Morán, F., 1993. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Engineering 6, 383-390.
3. Ausubel, F., Brent, R., Kingston, R., Moore, D., Seidman, J.G., Smith, J.A., Struhl, K., 1995. Short Protocols in Molecular Biology, third ed. Wiley, New York. pp. 10-38..
4. Barriocanal, J.G., Bonifacino, J.S., Yuan, L., Sandoval, I.V., 1986. Biosynthesis, glycosylation, movement through the Golgi system and transport to lysosomes by an N-linked carbohydrate-independent mechanism of three lysosomal integral membrane proteins. Journal of Biological Chemistry 261, 16755-16763.
5. Buffard, D., Breda, C., van Huystee, R.B., Asemota, O., Pierre, M., Dan Ha, D.B., Esnault, R., 1990. Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells. Proceedings of the National Academy of Science 87, 8874-8878.
6. Childs, R.E., Bardsley, W.G., 1975. The steady-state kinetics of peroxidase with 2,2′-azino-di-(3-ethy-benzthiazolin-6-sulphonic acid) as chromogen. Biochemical Journal 145, 93-103.
7. Cornish-Bowden, A., 1995. Fundamentals of enzyme kinetics. Portland Press, Colchester, UK. pp. 19-54.
8. Duarte-Vázquez, M.A., García-Almendarez, B., Regalado, C., Whitaker, J.R., 2001. Purification and properties of a neutral peroxidase from turnip (Brassica napus L var purple top white globe) roots. Journal of Agricultural and Food Chemistry 49, 4450-4456.
9. Dubois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A., Smith, F., 1956. Colorimetric method for determination of sugar and related substances. Analytical Chemistry 28, 350-356.
10. Dwek, R.A., 1996. Glycobiology: toward understanding the function of sugars. Chemical Reviews 96, 683-720.
11. Edge, A.S.B., Faltynek, C.R., Hof, L., Reichert, L.E., Weber, P., 1981. Deglycosylation of glycoproteins by trifluoromethanesulfonic acid. Analytical Biochemistry 118, 131-137.
12. Freeze, H.H., 2000. Endoglycosidase and glycoamidase release of N-linked oligosaccharides. In: Colligan, J.E., Dunn, B.M., Ploegh, H.N., Speicher, D.W., Wingfield, P.T. (Eds.), Current Protocols in Protein Science, Vol. 2. John Wiley, New York, pp. 12.4.1-12.4.6.
13. Gerard, C., 1990. Purification of glycoproteins. In: Deutscher, M.P. (Ed.), Guide to Protein Purification. Academic Press, San Diego, pp. 535-536.
14. Hecht, H.J., Kalisz, H.M., Hendle, J., Schmid, R.D., Shomburg, D., 1993. Crystal structure of glucose oxidase from Aspergillus niger refined at 23 angstrom resolution. Journal of Molecular Biology 229, 153-172.
15. Henriksen, A., Welinder, K.G., Gajhede, M., 1998. Structure of barley grain peroxidase refined at 19-Å resolution. A plant peroxidase reversible inactivated at neutral pH. Journal of Biological Chemstry 273, 2241-2248.
16. Hu, C., van Huystee, R.B., 1989a. Role of carbohydrate moieties in peanut (Arachis hypogaea) peroxidases. Biochemical Journal 263, 129-135.
17. Hu, C., van Huystee, R.B., 1989b. Immunochemical relatedness of two peroxidase isozymes from peanut cell culture. Biochemistry and Cell Biology 67, 371-376.
18. Jacob, L., Lety, M.A., Back, J.F., Louvard, D., 1986. Human systemic lupus erythematosus sera contain antibodies against cell-surface protein(s) that share(s) epitope(s) with DNA. Proceedings of the National Academy of Science 83, 6970-6974.
19. Kim, S.H., Kim, S.S., 1995. Carbohydrate moieties of three radish peroxidases. Phytochemistry 42, 287-290.
20. Kurosaka, A., Yano, A., Itoh, N., Kuroda, Y., Nakagawa, T., Kawasaki, T., 1991. The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum. Journal of Biological Chemistry 266, 4168-4172.
21. Lige, B., Ma, S., van Huystee, R.B., 2001. The effects of the site-directed removal of N-glycosylation from cationic peanut peroxidase on its function. Archives of Biochemistry and Biophysics 386, 17-24.
22. Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
23. McManus, M.T., McKeating, J., Secher, D.S., Osborne, D.J., Ashford, D.J., Dwek, R.A., Rademacher, T.W., 1988. Identification of a monoclonal antibodies to abscission tissue that recognizes xylose/fucose-containing N-linked oligosaccharides from higher plants. Planta 175, 506-512.
24. Manavalan, P., Johnson, C., 1983. Sensitivity if circular dichroism to protein tertiary structure class. Nature 305, 831-832.
25. Marcone, M.F., Yada, R.Y., 1997. Evidence for the phosphorylation and glycosylation of the amaranth 11S globulin (amaranthin). Journal of Food Biochemistry 21, 341-369.
26. Nicell, J.A., Wright, H., 1997. A model of peroxidase activity with inhibition by hydrogen peroxidase. Enzyme and Microbial Technology 21, 302-310.
27. Nie, G., Reading, S.N., Aust, S., 1999. Relative stability of recombinant versus native peroxidase from Phanerochaete chrysosporium. Archives of Biochemistry and Biophysics 365, 328-334.
28. Rademacher, T.W., Parekh, R.B., Dwek, R.A., 1988. Glycobiology. Annual Review of Biochemistry 57, 785-838.
29. Sánchez-Romero, C., García-Gómez, M.L., Pliego-Alfaro, F., Heredia, A., 1994. Effect of partial deglycosylation on catalytic characteristics and stability of an avocado peroxidase. Physiologia Plantarum 92, 97-101.
30. Schmitz, N., Gijzen, M., van Huystee, R., 1997. Characterization of anionic soybean (Glycine max) seed coat peroxidase. Canadian Journal of Botany 75, 1336-1341.
31. Schwarz, R.T., Datema, R., 1982. Inhibition of the dolichol pathway of protein glycosylation. In: Ginsburg, V. (Ed.), Methods in Enzymology Vol. 83. Complex Carbohydrates part D, pp. 432-443.
32. Schuller, D.J., Ban, N., van Huystee, R.B., McPherson, A., Poulus, T.L., 1996. The crystal structure of peanut peroxidase. Structure 4, 311-321.
33. 1H-NMR spectroscopy. Phytochemistry 53, 135-144.
34. Smith, P.K., Krohn, R.I., Hermanson, G.T., Mallia, A.K., Gartner, F.H., Provenzano, M.D., Fujimoto, E.K., Goeke, N.M., Olson, B.J., Klenk, D.C., 1985. Measurement of protein using bicinchoninic acid. Analytical Biochemistry 150, 76-85.
35. Sun, Y., Lige, B., van Huystee, R.B., 1997. HPLC determination of the sugar compositions of the glycans on the cationic peanut peroxidase. Journal of Agricultural and Food Chemistry 45, 4196-4200.
36. Tams, J.W., Welinder, K.G., 1995. Mild chemical deglycosylation of horseradish peroxidase yields a fully active, homogeneous enzyme. Analytical Biochemistry 228, 48-55.
37. Tigier, H.A., Quesada, M.A., Heredia, A., Valpuesta, V., 1991. Partial deglycosylation of an anionic isoperoxidase from peach seeds. Effect on enzymatic activity, stability and antigenicity. Physiologia Plantarum 83, 144-148.
38. Vaitukaitis, J., Robbins, J., Nieschlag, E., Ross, G.T., 1971. A method for producing specific antisera with small doses of immunogen. Journal of Clinical Endocrinology 33, 988-991.
39. Varki, A., 1993. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3, 97-130.
40. Wan, L., van Huystee, R.B., 1994. Immunogenicity of the N-glycans of peanut peroxidase. Phytochemistry 37, 933-940.
41. Wang, C., Eufemi, M., Turano, C., Giartosio, A., 1996. Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry 35, 7299-7307.
42. Wasserman, B.P., Hultin, H.O., 1981. Effect of deglycosylation on the stability of Aspergillus niger catalase. Archives of Biochemistry and Biophysics 212, 385-392.
43. Welinder, K.G., 1985. Plant peroxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidase. European Journal of Biochemistry 151, 497-504.
44. Yasuda, Y., Takahashi, N., Murachi, T., 1971. Periodate oxidation of carbohydrate moiety of bromelain without much alteration in activity. Biochemical Journal 10, 1624-1630.