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Chitin-binding protein

Fig. 3. The scheme of the precipitates formed by the crude protein extracts of plants of the groups monocotyledons (1-11, table 1) and dicotyledons (12-23 table 1) with antibodies against wheat chitin-binding proteins (I) and with antibodies against wheat anionic PO (H). Fig. 3. The scheme of the precipitates formed by the crude protein extracts of plants of the groups monocotyledons (1-11, table 1) and dicotyledons (12-23 table 1) with antibodies against wheat chitin-binding proteins (I) and with antibodies against wheat anionic PO (H).
J. J. Beintema, Structural features of plant chitinases and chitin-binding proteins, FEES Lett., 350 (1994) 159-163. [Pg.348]

W. F. Broekaert, W. Marien, F. R. Terras, M. F. De Bolle, P. Proost, J. van Damme, L. Dillen, M. Claeys, S. B. Rees, and J. Vanderleyden, Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine glycine rich domain of chitin-binding proteins. Biochemistry, 31 (1992) 4308-4314. [Pg.348]

N. V. Raikhel and H. I. Lee, Structure and function of chitin-binding proteins, Annu. Rev. Plant Physiol. Plant Mol. Biol, 44 (1993) 591-615 M. el Bouyoussfi, G. Laus, P. Verheyden,... [Pg.348]

Z. Shen and M. Jacobs-Lorena, Evolution of chitin-binding proteins in invertebrates, J. Mol. EvoL, 48 (1999) 341-347. [Pg.354]

T. Suetake, S. Tsuda, S. Kawabata, K. Miura, S. Iwanaga, K. Hikichi, K. Nitta, and K. Kawano, Chitin-binding proteins in invertebrates and plants comprise a common chitin-bind-ing structural motif, J. Biol. Chem., 275 (2000) 17929-17932. [Pg.354]

The bacterium, Serratia marcescens, is one of the most extensively studied multiple chitinases producer (Horn et al. 2006 Suzuki et al. 2002 Vaaje-Kolstad et al. 2005). This bacterium possesses three chitinases ChiA, ChiB, and ChiC, as well as one chitin-binding protein CBP21. ChiC often occurs in two forms in cultures of this bacterium the complete protein, sometimes called ChiCl, and a proteolytically truncated variant, called ChiC2, which lacks the two putative chitin-binding domains. ChiC is suggested as an endo-chitinase and degrade chitin in a nonprogressive mode. [Pg.187]

Vaaje-Kolstad, G., Horn, S. J., van Aalten, D. M., Synstad, B., and Eijsink, V. G. 2005. The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation. J Biol Chem 280 28492-28497. [Pg.192]

Matsuda Y, Koshiba T., Osaki T. et al. 2007. An arthropod cuticular chitin-binding protein endows injured sites with transglutaminase-dependent mesh. J Biol Chem 282 37316-37324. [Pg.401]

PRUZZO c, CRIPPA A, BERTONE s, PANE L and CARU A (1996) Attachment of Vibrio alginolyticus to chitin mediated by chitin-binding proteins. Microbiology-UK, 142, 2181-2186. [Pg.244]

Vaaje-Kolstad, G Horn, SJ van Aalten, DMF Synstad, B Eijsink, VGH. The Non-cataiytic Chitin-binding Protein CBP21 from Serratia marcescens Is Essentiai for Chitin Degradation. The Journal of Biological Chemistry, 2005, 280(31), 28492-7. [Pg.917]


See other pages where Chitin-binding protein is mentioned: [Pg.365]    [Pg.51]    [Pg.487]    [Pg.2357]    [Pg.320]    [Pg.408]    [Pg.306]    [Pg.238]    [Pg.706]    [Pg.187]    [Pg.723]    [Pg.173]    [Pg.179]    [Pg.345]   
See also in sourсe #XX -- [ Pg.8 , Pg.51 , Pg.487 , Pg.489 , Pg.504 ]




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