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김영식,이미연,박영목 ( Yeong Shik Kim,Mi Youn Lee,Young Mok Park ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.2
Chitinase (EC 3.2.1.14) was purified from the mature tissue of green onion by ammonium sulfate precipitation followed by affinity chromatography on a regenerated chitin and a Sephacryl HR-100. The purified enzyme gave a single band on polyacrylamide slab gel electrophoresis and its molecular weight was determined to be 35,000 Da using SDS-PAGE and HPLC-GPC. The isoelectric points of the enzyme were 3.5 and 7.2. The purified enzyme was stable on incubation at 50℃ for up to 20 min. Most of metal ions did not affect the activity significantly except that Ag^+ and Hg^(2+) ions inhibited the enzyme activity at 10 mM concentration. HPLC analysis of the initial products from the digestion of colloidal chitin and chitooligosaccharides indicated that chitinase was endolytic in action, yielding oligomers from the dimer to higher oligosaccharides.