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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

Andrade M H, Silva E, Mares-Guia M

Departamento de Bioquímica e Imunologia, Universidade Federal de Minas Gerais, Belo Horizonte, Brasil.

Braz J Med Biol Res. 1990;23(12):1223-31.

The determination of the binding of 4,4'-diazoamino-bis-benzamidine (DABB) to alpha-trypsin by equilibrium measurements in columns indicated a stoichiometry of 2 mol ligand/mol enzyme. One molecule of ligand is bound to the active center, as shown by competitive experiments and Ki. The second molecule binds to the secondary binding site, with Ki2 = 0.63 mM at pH 8.0, 25 degrees C. 2. Bovine pancreatic trypsin inhibitor (BPTI) prevented binding of DABB to both sites, indicating that they are topographically close and within the interface of the trypsin-BPTI complex. 3. On the basis of data from the literature regarding the tertiary structure of the trypsin-BPTI complex, we concluded that the secondary binding site of trypsin is plausibly identified as the same site in trypsin that binds the Arg-17 residue of BPTI, i.e., Tyr-39 and Tyr-151 in bovine trypsin. This site would then correspond to subsite S'2 on the enzyme surface.

通过柱平衡测量法测定4,4'-重氮氨基双苯甲脒（DABB）与α-胰蛋白酶的结合情况，结果表明配体与酶的化学计量比为2摩尔配体/摩尔酶。如竞争实验和抑制常数（Ki）所示，一个配体分子结合到活性中心。第二个分子结合到二级结合位点，在pH 8.0、25℃条件下，其抑制常数Ki2 = 0.63 mM。2. 牛胰蛋白酶抑制剂（BPTI）可阻止DABB与两个位点的结合，这表明这两个位点在拓扑结构上相近，且位于胰蛋白酶 - BPTI复合物的界面内。3. 根据文献中有关胰蛋白酶 - BPTI复合物三级结构的数据，我们得出结论，胰蛋白酶的二级结合位点可能与胰蛋白酶中结合BPTI的精氨酸 - 17残基的位点相同，即在牛胰蛋白酶中为酪氨酸 - 39和酪氨酸 - 151。该位点随后将对应于酶表面的S'2亚位点。

Andrade M H, Silva E, Mares-Guia M

Departamento de Bioquímica e Imunologia, Universidade Federal de Minas Gerais, Belo Horizonte, Brasil.

Braz J Med Biol Res. 1990;23(12):1223-31.

The determination of the binding of 4,4'-diazoamino-bis-benzamidine (DABB) to alpha-trypsin by equilibrium measurements in columns indicated a stoichiometry of 2 mol ligand/mol enzyme. One molecule of ligand is bound to the active center, as shown by competitive experiments and Ki. The second molecule binds to the secondary binding site, with Ki2 = 0.63 mM at pH 8.0, 25 degrees C. 2. Bovine pancreatic trypsin inhibitor (BPTI) prevented binding of DABB to both sites, indicating that they are topographically close and within the interface of the trypsin-BPTI complex. 3. On the basis of data from the literature regarding the tertiary structure of the trypsin-BPTI complex, we concluded that the secondary binding site of trypsin is plausibly identified as the same site in trypsin that binds the Arg-17 residue of BPTI, i.e., Tyr-39 and Tyr-151 in bovine trypsin. This site would then correspond to subsite S'2 on the enzyme surface.

通过柱平衡测量法测定4,4'-重氮氨基双苯甲脒（DABB）与α-胰蛋白酶的结合情况，结果表明配体与酶的化学计量比为2摩尔配体/摩尔酶。如竞争实验和抑制常数（Ki）所示，一个配体分子结合到活性中心。第二个分子结合到二级结合位点，在pH 8.0、25℃条件下，其抑制常数Ki2 = 0.63 mM。2. 牛胰蛋白酶抑制剂（BPTI）可阻止DABB与两个位点的结合，这表明这两个位点在拓扑结构上相近，且位于胰蛋白酶 - BPTI复合物的界面内。3. 根据文献中有关胰蛋白酶 - BPTI复合物三级结构的数据，我们得出结论，胰蛋白酶的二级结合位点可能与胰蛋白酶中结合BPTI的精氨酸 - 17残基的位点相同，即在牛胰蛋白酶中为酪氨酸 - 39和酪氨酸 - 151。该位点随后将对应于酶表面的S'2亚位点。