Abstract
Attempts to purify the inhibitor of pectin methylesterase (PMEI) from the soluble extract of ripe apricot (Prunus armeniaca) fruit led to isolation of a protein (Pa-INH) similar to PMEI, but having invertase inhibitory activity against vacuolar invertase from tomato. The molecular charge, the native and SDS-PAGE molecular weights were similar to those of PMEI. Partial amino acid sequence indicated a high level of identity with invertase inhibitors and a significant identity with PMEI. Circular dichroism analysis showed a mainly α-helix secondary structure for both the inhibitors and a higher thermostability of Pa-INH. Four Cys residues forming disulfide bridges in PMEI were conserved in Pa-INH. Similarly to PMEI, these residues were linked by disulfide bridges (first to second and third to fourth). The free Cys139 of PMEI is substituted by Ala in Pa-INH. The results reported in this study suggest a common structural arrangement of the two inhibitors.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
REFERENCES
Balestrieri, C., Castaldo, D., Giovane, A., Quagliuolo, L., and Servillo, L. (1990). Eur. J. Biochem. 193: 183–187.
Bracho, G. E., and Whitaker, J. R. (1990). Plant Physiol. 92: 386–394.
Camardella, L., Carratore, V., Ciardiello, M. A., Damonte, G., Benatti, U., and De Flora, A. (1995). Blood 85: 264–267.
Camardella, L., Carratore, V., Ciardiello, M. A., Servillo, L., Balestrieri, C., and Giovane, A. (2000). Eur. J. Biochem. 267: 4561–4565.
Giovane, A., Balestrieri, C., Quagliuolo, L., Castaldo, D., and Servillo, L. (1995). Eur. J. Biochem. 233: 926–929.
Greiner, S., Krausgrill, S., and Rausch, T. (1998). Plant Physiol. 116: 733–742.
Greiner, S., Rausch, T., Sonnewald, U., and Herbers, K. (1999). Nat. Biotechnol. 17: 708–711.
Greiner, S., Koster, U., Lauer, K., Rosenkranz, H., Vogel, R., and Rausch, T. (2000). Aust. J. Plant Physiol. 27: 807–814.
Isla, M. I., Vattuone, M. A., Gutierrez, M. I., and Sampietro, A. R. (1991). Phytochemistry 27: 1993–1998.
Jaynes, T. A., and Nelson, O. E. (1971). Plant Physiol. 47: 629–634.
Matsushita, K., and Uritani, I. (1976). J. Biochem. 79: 633–639.
Ovalle, R., Keyes, A. C., Ewing, E. E., and Quimby, F. W. (1995). J. Plant Physiol. 147: 334–340.
Pressey, R. (1966). Arch. Biochem. Biophys. 113: 667–674.
Pressey, R. (1968). Plant Physiol. 43: 1430–1434.
Pressey, R. (1994). Phytochemistry 36: 543–546.
Schwimmer, S., Makower, R. U., and Rorem, E. S. (1961). Plant Physiol. 36: 313–316.
Smeekens, S. (1998). Curr. Opin. Plant Biol. 1: 230–234.
Sturm, A. (1999). Plant Physiol. 121: 1–7.
Weil, M., Krausgrill, S., Schuster, A., and Rausch, T. (1994). Planta 193: 438–445.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Scognamiglio, M.A., Ciardiello, M.A., Tamburrini, M. et al. The Plant Invertase Inhibitor Shares Structural Properties and Disulfide Bridges Arrangement with the Pectin Methylesterase Inhibitor. J Protein Chem 22, 363–369 (2003). https://doi.org/10.1023/A:1025342207831
Published:
Issue Date:
DOI: https://doi.org/10.1023/A:1025342207831