Takahashi T, Nishibe H
Biochim Biophys Acta. 1981 Feb 13;657(2):457-67. doi: 10.1016/0005-2744(81)90331-4.
The glycopeptidase preparation that has been isolated from almond emulsin and acts on beta-aspartylglycosylamine linkages in glycopeptides was separated into three active fractions by DEAE-cellulose column chromatography. The three discrete species of glycopeptidase (Groups A, B and C) have been purified 30-, 136-, and 99-fold, respectively. The optimum pH value of Group A was 6.0 and those of Groups B and C, 5.0. Isoelectric points of Groups A, B and C were pH 7.7, 8.6 and 8.7, respectively. All three glycopeptidases hydrolyzed quantitatively glycopeptides with 3-11 amino acid residues prepared from stem bromelain, ovalbumin and ovotransferrin. Group C preferred glycopeptides with shorter peptide chains, whereas Groups A and B preferred those with longer chains. Glycopeptidase Group A also hydrolyzed intact glycoproteins such as stem bromelain, ovalbumin, Taka-amylase A and desialylated human transferrin.
从杏仁苦苷酶中分离得到的、作用于糖肽中β-天冬氨酰糖胺键的糖肽酶制剂，通过DEAE-纤维素柱色谱法被分离成三个活性组分。三种不同的糖肽酶（A组、B组和C组）分别被纯化了30倍、136倍和99倍。A组的最适pH值为6.0，B组和C组的最适pH值为5.0。A组、B组和C组的等电点分别为pH 7.7、8.6和8.7。所有三种糖肽酶都能定量水解由菠萝蛋白酶、卵清蛋白和卵转铁蛋白制备的含有3至11个氨基酸残基的糖肽。C组更喜欢肽链较短的糖肽，而A组和B组更喜欢肽链较长的糖肽。A组糖肽酶还能水解完整的糖蛋白，如菠萝蛋白酶、卵清蛋白、高峰淀粉酶A和去唾液酸人转铁蛋白。
