Purification and characterization of a XIP-type endoxylanase inhibitor from rice (Oryza sativa).

@article{Goesaert2005PurificationAC,
  title={Purification and characterization of a XIP-type endoxylanase inhibitor from rice (Oryza sativa).},
  author={Hans Goesaert and Kurt Gebruers and Christophe M Courtin and Jan A Delcour},
  journal={Journal of enzyme inhibition and medicinal chemistry},
  year={2005},
  volume={20 1},
  pages={95-101}
}
A rice XIP-type inhibitor was purified by affinity chromatography with an immobilized Aspergillus aculeatus family 10 endoxylanase. Rice XIP is a monomeric protein, with a molecular mass of ca. 32 kDa and a pI of ca. 5.6. Its N-terminal amino acid sequence was identical to that of a rice chitinase homologue, demonstrating the difficulty when using sequence information to differentiate between endoxylanase inhibitors and (putative) chitinases in rice. Rice XIP inhibited different endoxylanases… CONTINUE READING
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