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首页> 外文期刊>The biochemical journal >Cleavage by trypsin and by the proteinase from Armillaria mellea at ?-N-formyl-lysine residues
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Cleavage by trypsin and by the proteinase from Armillaria mellea at ?-N-formyl-lysine residues

机译:用胰蛋白酶和蜜环菌的蛋白酶在α-N-甲酰基-赖氨酸残基处进行切割

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pKinetic studies were made of the hydrolysis by trypsin of alpha-N-acetylglycyl-L-lysine methyl ester and of its neutral analogue alpha-N-acetylglycyl-epsilon-N-formyl-L-lysine methyl ester. The latter substance is a moderately good substrate for trypsin, and this observation is discussed in terms of the substrate specifically of the enzyme. The actions of trypsin and of the lysine-specific proteinase from Armillaria mellea on both a native and a formylated polypeptide substrate were compared. Both enzymes were found to hydrolyse specifically bonds to epsilon-N-formyl-lysine in the formylated substrate./p
机译:胰蛋白酶对α-N-乙酰基乙酰基-L-赖氨酸甲酯的胰蛋白酶水解进行了动力学研究。后一种物质是胰蛋白酶的中等良好的底物,并且针对该酶的底物进行了讨论。比较了胰蛋白酶和来自蜜环蜜环菌的赖氨酸特异性蛋白酶对天然和甲酰化多肽底物的作用。发现这两种酶都可以水解甲酰化底物中的ε-N-甲酰基-赖氨酸。

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