Isolation of two endo-β-N-acetylglucosaminidases from fig latex

Su-Chen Li, Makio Asakawa, Yoshio Hirabayashi, Yu-Teh Li
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引用次数: 11

Abstract

Two endo-β-N-acetylglucosaminidases (mannosyl-glycoprotein 1,4-N-acetamidodeoxy-β-d-glycohydrolase, EC 3.2.1.96) (type F-I and type F-II) have been isolated from fig latex. At pH 7.0, type F-1 was retained by the DEAE-Sephadex A-50 column, whereas type F-II was not adsorbed by the column. The optimum pH of type F-I was found to be pH 5.9 and type F-II, pH 5.4. Type F-I enzyme hydrolyzes the tri-mannosyl derivatives di-N-acetylglucosaminylasparagine faster than the penta- or hexa-mannosyl compounds. Type F-II hydrolyzes the penta- and hexa-mannosyl derivatives, but not the tri-mannosyl compound.

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无花果胶乳中两个内端-β- n -乙酰氨基葡萄糖酶的分离
从无花果乳胶中分离到两个内切-β- n -乙酰氨基葡萄糖氨基酶(甘露糖糖蛋白1,4- n -乙酰氨基脱氧-β-d-糖水解酶,EC 3.2.1.96) (F-I型和F-II型)。在pH 7.0时,型F-1被DEAE-Sephadex A-50柱保留,而型F-II不被柱吸附。F-I型的最佳pH为5.9,F-II型的最佳pH为5.4。F-I型酶水解三甘露糖基衍生物二n -乙酰氨基葡萄糖天冬氨酸的速度比五甘露糖基或六甘露糖基化合物快。F-II型水解五甘露糖基和六甘露糖基衍生物,但不能水解三甘露糖基化合物。
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