Baskova I P, Nikonov G I, Zavalova L L, Larionova N I
Biokhimiia. 1990 Apr;55(4):674-9.
The molecular mass of destabilase isolated from the medicinae leech Hirudo medicinalis was found to be equal to 12.3 kDa. A kinetic analysis of the sole presently known synthetic substrate, L-gamma-Glu-pNA, showed that the enzyme is relatively stable to heating (5 min, 70 degrees C); the pH optimum lies at 7.0-8.5. The enzyme has a specific activity of 0.15 x 10(-9) mol.s-1.mg-1; Km = 2.2 x 10(-4) M, kcat is 3.53 x 10(-3) s-1 (pH 8.0, 37 degrees C).
从医用水蛭药用水蛭中分离出的去稳定酶的分子量被发现等于12.3 kDa。对目前已知的唯一合成底物L-γ-谷氨酰对硝基苯胺的动力学分析表明，该酶对加热相对稳定（5分钟，70摄氏度）；最适pH值在7.0 - 8.5之间。该酶的比活性为0.15×10⁻⁹ mol·s⁻¹·mg⁻¹；Km = 2.2×10⁻⁴ M，kcat为3.53×10⁻³ s⁻¹（pH 8.0，37摄氏度）。
