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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

Bonaccorsi di Patti M C, Galtieri A, Giartosio A, Musci G, Calabrese L

Department of Biochemical Sciences, University of Rome La Sapienza, Italy.

Comp Biochem Physiol B. 1992 Sep;103(1):183-8. doi: 10.1016/0305-0491(92)90429-u.

Ceruloplasmin, the blue protein of the plasma of vertebrates, was isolated from dolphin, a marine mammal. The protein showed overall physico-chemical parameters very similar to those of all other mammalian ceruloplasmins. The spectroscopic properties indicated a conservation of the copper binding sites. 2. Non-denaturing electrophoresis revealed a conformation similar to that of other mammalian ceruloplasmins. EPR spectroscopy and calorimetric analyses indicated a three-domain arrangement of the protein typical of "aged" ceruloplasmin. 3. Dolphin ceruloplasmin is the only mammalian ceruloplasmin insensitive to trypsin, plasmin or chymotrypsin. This property, however, does not result in a higher conformational stability of the molecule. Thus, susceptibility of ceruloplasmin to aging is not directly related to the lability to proteases, which is typical of all other mammalian ceruloplasmins so far studied.

铜蓝蛋白是脊椎动物血浆中的蓝色蛋白质，从海洋哺乳动物海豚中分离得到。该蛋白质的整体物理化学参数与所有其他哺乳动物的铜蓝蛋白非常相似。光谱特性表明铜结合位点具有保守性。2. 非变性电泳显示其构象与其他哺乳动物铜蓝蛋白的构象相似。电子顺磁共振光谱和量热分析表明该蛋白质具有典型的“老化”铜蓝蛋白的三结构域排列。3. 海豚铜蓝蛋白是唯一对胰蛋白酶、纤溶酶或胰凝乳蛋白酶不敏感的哺乳动物铜蓝蛋白。然而，这一特性并未导致该分子具有更高的构象稳定性。因此，铜蓝蛋白对老化的敏感性与蛋白酶敏感性并无直接关系，而蛋白酶敏感性是迄今为止所研究的所有其他哺乳动物铜蓝蛋白的典型特征。

Bonaccorsi di Patti M C, Galtieri A, Giartosio A, Musci G, Calabrese L

Department of Biochemical Sciences, University of Rome La Sapienza, Italy.

Comp Biochem Physiol B. 1992 Sep;103(1):183-8. doi: 10.1016/0305-0491(92)90429-u.

Ceruloplasmin, the blue protein of the plasma of vertebrates, was isolated from dolphin, a marine mammal. The protein showed overall physico-chemical parameters very similar to those of all other mammalian ceruloplasmins. The spectroscopic properties indicated a conservation of the copper binding sites. 2. Non-denaturing electrophoresis revealed a conformation similar to that of other mammalian ceruloplasmins. EPR spectroscopy and calorimetric analyses indicated a three-domain arrangement of the protein typical of "aged" ceruloplasmin. 3. Dolphin ceruloplasmin is the only mammalian ceruloplasmin insensitive to trypsin, plasmin or chymotrypsin. This property, however, does not result in a higher conformational stability of the molecule. Thus, susceptibility of ceruloplasmin to aging is not directly related to the lability to proteases, which is typical of all other mammalian ceruloplasmins so far studied.

铜蓝蛋白是脊椎动物血浆中的蓝色蛋白质，从海洋哺乳动物海豚中分离得到。该蛋白质的整体物理化学参数与所有其他哺乳动物的铜蓝蛋白非常相似。光谱特性表明铜结合位点具有保守性。2. 非变性电泳显示其构象与其他哺乳动物铜蓝蛋白的构象相似。电子顺磁共振光谱和量热分析表明该蛋白质具有典型的“老化”铜蓝蛋白的三结构域排列。3. 海豚铜蓝蛋白是唯一对胰蛋白酶、纤溶酶或胰凝乳蛋白酶不敏感的哺乳动物铜蓝蛋白。然而，这一特性并未导致该分子具有更高的构象稳定性。因此，铜蓝蛋白对老化的敏感性与蛋白酶敏感性并无直接关系，而蛋白酶敏感性是迄今为止所研究的所有其他哺乳动物铜蓝蛋白的典型特征。