J Integr Plant Biol. ›› 1994, Vol. 36 ›› Issue (11): -.
• Research Articles •
Shi Yi min, Yan Ji qiong, Fei Xue nan and Xu Yu quan
Abstract: Some properties of the β-N-acetyl-D-hexosaminidase purified from intercellular fluid of tomato leaves after the plant was systematically infected by TMV (tobacco mosaic virus) were studied. When pNP β-D-GlcNAc (p nitrophenyl-N-aeetyl β-D-glucosaminide) or pNP β-D- GalNAc (p-nitrophenyl-N-acetyl-β-D galactosaminide) was used as the substrate, it showed the optical pH between 4. 8--5.0 and optical temperature between 44— 47℃. Studies of thermostabillty indicated that the enzyme had a biphasic denaturation curve. Using pNP-β-D-GIcNAc or pNP-β-D GalNAc as the substrate, the Km value of the enzyme was 0. 36 and 0. 67 mmol/L respectively. N acetyi-D glucosamine and N acetyl-D-galactosamine were competitive inhibitors of the enzyme activities. Ag+ and Hg2+ were sensitive inhibitors and Fe2+ . Fe3+ and Cu2+ were also inhibitors enzyme activities.
Key words: Key words Tomato, Tobacco mosaic virus, β-N-Acetyl-D-hexosaminidase
Shi Yi min, Yan Ji qiong, Fei Xue nan and Xu Yu quan. Studies on Some Properties of the Apoplastic β-N-Acetyl-D-Hexosaminidase from Tomato Leaves[J]. J Integr Plant Biol., 1994, 36(11): -.
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