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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Biochim Biophys Acta. 1975 Aug 26;397(2):437-42. doi: 10.1016/0005-2744(75)90133-3.

The enzyme activity in the particulate fraction from rat liver that hydrolyzes alpha-N-benzoyl-DL-arginine-2-naphthylamide (Bz-Arg-NNap) has been separated into two approximately equal components by chromatography on DEAE-cellulose. One component (peak II) is completely retained by the column at low ionic strength while the other component (peak I) passes through. 2. In contrast to the enzyme in peak I, the enzyme in peak II is extremely sensitive to inhibition by leupeptin, it will hydrolyze carbobenzoxy-alanylarginylarginyl-4-methoxy-2-naphthylamine, and it will inactivate aldolase. 3. There appears to be also a minor high molecular weight component of the alpha-N-benzoyl-DL-arginyl-2-naphthylamine-hydrolyzing activity that is retained by the DEAE-cellulose but which has properties similar to those of the peak I enzyme.

大鼠肝脏微粒体部分中水解α-N-苯甲酰-DL-精氨酸-2-萘酰胺（Bz-Arg-NNap）的酶活性，通过在DEAE-纤维素上进行色谱分离，已被分成两个大致相等的组分。一个组分（峰II）在低离子强度下被柱完全保留，而另一个组分（峰I）则通过柱子。2. 与峰I中的酶相反，峰II中的酶对亮抑酶肽的抑制极其敏感，它能水解苄氧羰基-丙氨酰精氨酰精氨酰-4-甲氧基-2-萘胺，并且能使醛缩酶失活。3. 似乎还存在一种水解α-N-苯甲酰-DL-精氨酰-2-萘胺活性的次要高分子量组分，它被DEAE-纤维素保留，但具有与峰I酶相似的性质。

Biochim Biophys Acta. 1975 Aug 26;397(2):437-42. doi: 10.1016/0005-2744(75)90133-3.

The enzyme activity in the particulate fraction from rat liver that hydrolyzes alpha-N-benzoyl-DL-arginine-2-naphthylamide (Bz-Arg-NNap) has been separated into two approximately equal components by chromatography on DEAE-cellulose. One component (peak II) is completely retained by the column at low ionic strength while the other component (peak I) passes through. 2. In contrast to the enzyme in peak I, the enzyme in peak II is extremely sensitive to inhibition by leupeptin, it will hydrolyze carbobenzoxy-alanylarginylarginyl-4-methoxy-2-naphthylamine, and it will inactivate aldolase. 3. There appears to be also a minor high molecular weight component of the alpha-N-benzoyl-DL-arginyl-2-naphthylamine-hydrolyzing activity that is retained by the DEAE-cellulose but which has properties similar to those of the peak I enzyme.

大鼠肝脏微粒体部分中水解α-N-苯甲酰-DL-精氨酸-2-萘酰胺（Bz-Arg-NNap）的酶活性，通过在DEAE-纤维素上进行色谱分离，已被分成两个大致相等的组分。一个组分（峰II）在低离子强度下被柱完全保留，而另一个组分（峰I）则通过柱子。2. 与峰I中的酶相反，峰II中的酶对亮抑酶肽的抑制极其敏感，它能水解苄氧羰基-丙氨酰精氨酰精氨酰-4-甲氧基-2-萘胺，并且能使醛缩酶失活。3. 似乎还存在一种水解α-N-苯甲酰-DL-精氨酰-2-萘胺活性的次要高分子量组分，它被DEAE-纤维素保留，但具有与峰I酶相似的性质。