用硫酸软骨素-4-衍生物对双阿司匹林交联血红蛋白（DCLHb）进行表面修饰。第1部分。
Surface modification of diaspirin cross-linked hemoglobin (DCLHb) with chondroitin-4-sulfate derivatives. Part 1.
作者信息
Hai T T, Pereira D E, Nelson D J, Catarello J, Srnak A
机构信息
Corporate Research and Technical Services, Baxter Healthcare Corporation, 25212 West State Route 120, Round Lake, Illinois 60073-9799, USA.
出版信息
Bioconjug Chem. 2000 Sep-Oct;11(5):705-13. doi: 10.1021/bc000021i.
Synthetic methodology was developed for the preparation of chondrotin-4-sulfate reagents that could be specifically attached to the surface of diaspirin cross-linked hemoglobin (DCLHb), a chemically stabilized human hemoglobin. The surface-modified hemoglobin solutions had a significantly higher colloidal osmotic pressures (COP) than DCLHb. The P(50) of the modified DCLHb was dependent upon the reactive end group of the chondrotin-4-sulfate reagents that was used for the protein modification. Modification of DCLHb with the chondroitin-4-sulfate derivatives containing the maleimide end group 23 provided a hemoglobin with a P(50) value of 23 mmHg, while the P(50) of hemoglobins prepared from chondroitin-4-sulfate derivatives containing the aldehyde end group 13 and 18 remained unchanged from that of DCLHb.
已开发出一种合成方法，用于制备可特异性连接到双阿司匹林交联血红蛋白（DCLHb，一种化学稳定的人血红蛋白）表面的硫酸软骨素-4-硫酸盐试剂。表面修饰的血红蛋白溶液的胶体渗透压（COP）明显高于DCLHb。修饰后的DCLHb的P(50)取决于用于蛋白质修饰的硫酸软骨素-4-硫酸盐试剂的反应性端基。用含有马来酰亚胺端基23的硫酸软骨素-4-硫酸盐衍生物修饰DCLHb，得到的血红蛋白的P(50)值为23 mmHg，而用含有醛端基13和18的硫酸软骨素-4-硫酸盐衍生物制备的血红蛋白的P(50)与DCLHb的P(50)保持不变。
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