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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

Silveira A M, Magalhães A, Diniz C R, de Oliveira E B

Departamento de Bioquímica e Immunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Brasil.

Int J Biochem. 1989;21(8):863-71. doi: 10.1016/0020-711x(89)90285-1.

The coagulating enzyme of the Lachesis muta muta venom was purified to homogeneity by a combination of a gel filtration in Sephadex G-100 and affinity chromatography on agarose-agmatine resin. 2. Several forms of the enzyme were prepared by isoelectric focusing with pIs ranging from 3.1 to 5.0; the asialoenzyme focused as a narrow band at pH 8.7. SDS-PAGE analysis of the purified enzyme revealed a single broad band with apparent Mr of 41-47 kDa. 3. The enzyme cleaves only fibrinopeptide A from fibrinogen; it does not activate factor XIII and is devoid of kallikrein-like activity. 4. Kinetic properties of the enzyme were determined for representative synthetic chromogenic substrates and inhibitors.

通过在Sephadex G - 100中进行凝胶过滤和在琼脂糖 - 胍丁胺树脂上进行亲和色谱相结合的方法，将矛头蝮蛇毒的凝血酶纯化至同质。2. 通过等电聚焦制备了几种酶形式，其等电点范围为3.1至5.0；去唾液酸酶在pH 8.7处聚焦为一条窄带。对纯化酶的SDS - PAGE分析显示出一条单一的宽带，表观分子量为41 - 47 kDa。3. 该酶仅从纤维蛋白原中裂解纤维蛋白肽A；它不激活因子XIII且没有激肽释放酶样活性。4. 针对代表性的合成显色底物和抑制剂测定了该酶的动力学性质。

Silveira A M, Magalhães A, Diniz C R, de Oliveira E B

Departamento de Bioquímica e Immunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Brasil.

Int J Biochem. 1989;21(8):863-71. doi: 10.1016/0020-711x(89)90285-1.

The coagulating enzyme of the Lachesis muta muta venom was purified to homogeneity by a combination of a gel filtration in Sephadex G-100 and affinity chromatography on agarose-agmatine resin. 2. Several forms of the enzyme were prepared by isoelectric focusing with pIs ranging from 3.1 to 5.0; the asialoenzyme focused as a narrow band at pH 8.7. SDS-PAGE analysis of the purified enzyme revealed a single broad band with apparent Mr of 41-47 kDa. 3. The enzyme cleaves only fibrinopeptide A from fibrinogen; it does not activate factor XIII and is devoid of kallikrein-like activity. 4. Kinetic properties of the enzyme were determined for representative synthetic chromogenic substrates and inhibitors.

通过在Sephadex G - 100中进行凝胶过滤和在琼脂糖 - 胍丁胺树脂上进行亲和色谱相结合的方法，将矛头蝮蛇毒的凝血酶纯化至同质。2. 通过等电聚焦制备了几种酶形式，其等电点范围为3.1至5.0；去唾液酸酶在pH 8.7处聚焦为一条窄带。对纯化酶的SDS - PAGE分析显示出一条单一的宽带，表观分子量为41 - 47 kDa。3. 该酶仅从纤维蛋白原中裂解纤维蛋白肽A；它不激活因子XIII且没有激肽释放酶样活性。4. 针对代表性的合成显色底物和抑制剂测定了该酶的动力学性质。