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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. 1977 Mar 28;491(1):121-8. doi: 10.1016/0005-2795(77)90047-2.

The binding of sodium n-dodecyl sulphate to trypsin and reduced trypsin has been measured by equilibrium dialysis at pH 3.5 and 5.5. 2. At pH 3.5 trypsin specifically binds surfactant at low concentration, at higher concentrations co-operative binding occurs. 3. Reduction of trypsin destroys the specific binding sites at pH 3.5. 4. At pH 5.5 both trypsin and reduced trypsin show only co-operative binding. 5. The interaction of sodium n-dodecyl sulphate with trypsin, reduced, inhibited, and thermally denatured trypsins has been studied by microcalorimetry at 25 degrees C. 6. The microcalorimetric measurements have been used to estimate enthalpy changes (deltaHd) on unfolding of trypsin; deltaHd = 82 +/- 5 kJ-mol-1 at pH 3.5 and 128 +/- 5 kJ-mol-1 at pH 5.5. 7. The unfolding of trypsin follows a different thermochemical pathway to that of reduced trypsin.

已通过在pH 3.5和5.5下的平衡透析法测定了正十二烷基硫酸钠与胰蛋白酶及还原型胰蛋白酶的结合情况。2. 在pH 3.5时，胰蛋白酶在低浓度下特异性结合表面活性剂，在较高浓度下会发生协同结合。3. 胰蛋白酶的还原作用会破坏pH 3.5时的特异性结合位点。4. 在pH 5.5时，胰蛋白酶和还原型胰蛋白酶均仅表现出协同结合。5. 已在25℃下通过微量量热法研究了正十二烷基硫酸钠与胰蛋白酶、还原型胰蛋白酶、抑制型胰蛋白酶及热变性胰蛋白酶的相互作用。6. 微量量热测量已用于估算胰蛋白酶展开时的焓变（ΔHd）；在pH 3.5时，ΔHd = 82±5 kJ·mol⁻¹，在pH 5.5时，ΔHd = 128±5 kJ·mol⁻¹。7. 胰蛋白酶的展开遵循与还原型胰蛋白酶不同的热化学途径。

Biochim Biophys Acta. 1977 Mar 28;491(1):121-8. doi: 10.1016/0005-2795(77)90047-2.

The binding of sodium n-dodecyl sulphate to trypsin and reduced trypsin has been measured by equilibrium dialysis at pH 3.5 and 5.5. 2. At pH 3.5 trypsin specifically binds surfactant at low concentration, at higher concentrations co-operative binding occurs. 3. Reduction of trypsin destroys the specific binding sites at pH 3.5. 4. At pH 5.5 both trypsin and reduced trypsin show only co-operative binding. 5. The interaction of sodium n-dodecyl sulphate with trypsin, reduced, inhibited, and thermally denatured trypsins has been studied by microcalorimetry at 25 degrees C. 6. The microcalorimetric measurements have been used to estimate enthalpy changes (deltaHd) on unfolding of trypsin; deltaHd = 82 +/- 5 kJ-mol-1 at pH 3.5 and 128 +/- 5 kJ-mol-1 at pH 5.5. 7. The unfolding of trypsin follows a different thermochemical pathway to that of reduced trypsin.

已通过在pH 3.5和5.5下的平衡透析法测定了正十二烷基硫酸钠与胰蛋白酶及还原型胰蛋白酶的结合情况。2. 在pH 3.5时，胰蛋白酶在低浓度下特异性结合表面活性剂，在较高浓度下会发生协同结合。3. 胰蛋白酶的还原作用会破坏pH 3.5时的特异性结合位点。4. 在pH 5.5时，胰蛋白酶和还原型胰蛋白酶均仅表现出协同结合。5. 已在25℃下通过微量量热法研究了正十二烷基硫酸钠与胰蛋白酶、还原型胰蛋白酶、抑制型胰蛋白酶及热变性胰蛋白酶的相互作用。6. 微量量热测量已用于估算胰蛋白酶展开时的焓变（ΔHd）；在pH 3.5时，ΔHd = 82±5 kJ·mol⁻¹，在pH 5.5时，ΔHd = 128±5 kJ·mol⁻¹。7. 胰蛋白酶的展开遵循与还原型胰蛋白酶不同的热化学途径。