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에틸렌이 유도한 강낭콩 잎 키틴분해효소의 정제 및 특성
박노동,이춘명,박남용 ( Ro Dong Park,Choon Myong Lee,Nam Yong Park ) 생화학분자생물학회 1991 BMB Reports Vol.24 No.2
Chitinase (EC 3.2.1.14), a potential pathogensis-related protein, was induced in leaves of 30-day-old bean (Phaseolus vulgaris) plants with treatment of 10 nl/ml ethylene for 30 hr. The enzyme was extracted in sodium citrate buffer (pH 5.0), and then purified by heat treatment, (NH₄)₂SO₄ precipitation, chitin-affinity and Sephadex G-75 chromatographies. Chitinase was enriched 22.5-fold with a yield of 29%. Its apparent molecular weight was estimated on SDS-PAGE to be 30 kD. Chitinase showed optimum pH 5.0 and broad pH stability, and showed thermal stability below 50℃. K_m and V_(max) values of the purified chitinase were 0.36 ㎎/㎖ and 0.7 nmole G1cNAc/min, respectively, for swollen chitin as a substrate. Chitinase was significantly inhibited by 10 mM Cu^(++), Hg^(++), S₂O₃^(--), S₂O₄^(--) or SO₃^(--) in reaction mixtures. Antibody was raised in rabbits against the chitinase and used for specific immunodetection of the enzyme.