The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Influence of the Carbohydrate Moiety on the Stability of Glycoproteins
Abstract
To study the role of oligosaccharides on the properties of glycoproteins, five glycoproteins (yeast external invertase, bovine serum fetuin, glucoamylase from Aspergillus niger, and chicken egg white ovotransferrin and avidin) of previously established glycan patterns were purified to homogeneity and deglycosylated with endo- and exo-glycosidases in native conditions. Thermal stability and conformational changes were measured by high-resolution differential scanning microcalorimetry and circular dicroism spectroscopy before and after they were deglycosylated. It was found that deglycosylation decreases protein thermal stability, as judged by the decrease in denaturation temperature and denaturation enthalpy, while it does not affect substantially the conformation as indicated by the CD spectra in the far UV range. The destabilization effect of deglycosylation seems to depend on the carbohydrate content, i.e., the maximum effect was observed for the most heavily glycosylated protein, irrespective of the types (N-linked or O-linked) or patterns (mono- or multi-branched) of the covalently attached carbohydrate chains. In addition, studies of the reversibility to heat denaturation revealed that deglycosylated proteins have a poorer thermal reversibility in calorimetric scans than their native counterparts and tend to aggregate during thermal inactivation at acidic pH. These results suggest that carbohydrate moieties, in addition to the apparent stabilizing effect, may prevent the unfolded or partially folded protein molecules from aggregation. Our results support the hypothesis that the general function of protein glycosylation is to aid in folding of the nascent polypeptide chain and in stabilization of the conformation of the mature glycoprotein.
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Cites
Kornfeld, S., & Mellman, I. (1989) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.05.110189.002411 · Cited by 1,580
Circular dichroic analysis of protein conformation: Inclusion of the β-turns
Chang, C. T., Wu, C.-S. C., & Yang, J. T. (1978) · Analytical Biochemistry · doi:10.1016/0003-2697(78)90812-6 · Cited by 1,089
Crystal Structure of Glucose Oxidase from Aspergillus niger Refined at 2·3 Å Reslution
Hecht, H. J., Kalisz, H. M., Hendle, J., Schmid, R. D., & Schomburg, D. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1015 · Cited by 676
Structure of the O-Glycosidically Linked Carbohydrate Units of Fetuin
Spiro, R. G., & Bhoyroo, V. D. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)79875-3 · Cited by 631
Biochemical Applications of Differential Scanning Calorimetry
Sturtevant, J. M. (1987) · Annual Review of Physical Chemistry · doi:10.1146/annurev.pc.38.100187.002335 · Cited by 607
Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells.
Moore, K. L., Stults, N. L., Diaz, S., Smith, D. F., Cummings, R. D., Varki, A., & McEver, R. P. (1992) · The Journal of cell biology · doi:10.1083/jcb.118.2.445 · Cited by 514
Carbohydrates as antigenic determinants of glycoproteins
Feizi, T., & Childs, R. A. (1987) · Biochemical Journal · doi:10.1042/bj2450001 · Cited by 264
Subunit structure of external invertase from Saccharomyces cerevisiae.
Trimble, R. B., & Maley, F. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40280-8 · Cited by 222
Studies on the attachment of carbohydrate to ovalbumin nascent chains in hen oviduct.
Kiely, M. L., McKnight, G. S., & Schimke, R. T. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33086-7 · Cited by 217
Trimble, R. B., Maley, F., & Chu, F. K. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32963-6 · Cited by 141
DORLAND, L., Haverkamp, J., Vliegenthart, J. F. G., et al. (1979) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1979.tb04203.x · Cited by 90
Gunnarsson, A., Svensson, B., Nilsson, B., et al. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08578.x · Cited by 82
Mellors, A., & Sutherland, D. R. (1994) · Trends in biotechnology · doi:10.1016/0167-7799(94)90006-x · Cited by 20
Cited by
Panel), E. P. O. G. M. O. (. (2010) · EFSA Journal · doi:10.2903/j.efsa.2010.1700 · Cited by 608
Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution
Moore, S. A., Anderson, B. F., Groom, C. R., Haridas, M., & Baker, E. N. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1386 · Cited by 419
Mimura, Y., Church, S., Ghirlando, R., Ashton, P. R., Dong, S., Goodall, M., Lund, J., & Jefferis, R. (2000) · Molecular Immunology · doi:10.1016/s0161-5890(00)00105-x · Cited by 329
Runkel, L., Meier, W., Pepinsky, R. B., Karpusas, M., Whitty, A., Kimball, K., Brickelmaier, M., Muldowney, C., Jones, W., & Goelz, S. E. (1998) · Pharmaceutical Research · doi:10.1023/a:1011974512425 · Cited by 304
Protein Native-State Stabilization by Placing Aromatic Side Chains in N-Glycosylated Reverse Turns
Culyba, E. K., Price, J. L., Hanson, S. R., Dhar, A., Wong, C.-H., Gruebele, M., Powers, E. T., & Kelly, J. W. (2011) · Science · doi:10.1126/science.1198461 · Cited by 171
Metadata
- Authors
- Wang, C., Eufemi, M., Turano, C., & Giartosio, A.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1996-01-01
- Volume
- 35
- Issue
- 23
- Pages
- 7299-7307
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2046714822
- Cited by
- 344
- References
- 13
- FWCI
- 4.95
- Type
- journal article
- Language
- en
- Open access
- closed
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