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KMID : 0578319930030030269
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Molecules and Cells
1993 Volume.3 No. 3 p.269 ~ p.274
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Purification and Characterization of Two Acidic Chitinases Having and Lacking N-Terminal Cysteine-rich Domain from Rood of Rice (Oryza sativa L.)
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Bae, Chang Gyu
Gal, Sang Wan/Kim, Cha young/Kang, Chang Ho/Hong, Jong chan/bahk, jeong Dong/lee, Sang Yeol
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Abstract
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Five chitinase isozymes with apparent molecular weight of 38, 36, 32, 31 and 28 kDa were detected from ´root of unstressed rice, from which 38 kDa (RACH i) and 31 kDa (RACH 11) chitinases were purified to homogeneity. Both RACH I and RACH 11 are acidic chitinases with a pI of approximately 3.8 as determined by isoelectric focusing. The former contains N-terminal cysteine-rich domain, whereas the latter lacks this sequence. Acidic chitinases have been known to be lacking in this sequence. The N-terminal 20 amino acid sequences of RACH I show considerable sequence similarity to the region of basic chitinases from other plant sources as well as wheat-germ agglutinin and hevein. RACH 1 shows strong antifungal activity against Trichoderma viride in vitro but does not inhibit the growth of several phytopathogenic fungi. RACH Ii does not affect the growth of all the fungi tested.
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