从人类胎儿中分离出的触珠蛋白-血红蛋白复合物的纯化与鉴定
Purification and characterization of a haptoglobin-hemoglobin complex isolated from human fetuses.
作者信息
Mucchielli A, Masseyeff R
出版信息
Oncodev Biol Med. 1981;2(6):371-80.
PMID:7346796
Abstract
A haptoglobin-hemoglobin complex was purified from human fetuses (10-week-old pregnancies). The yield was 12% and the purification factor was about 450. The purified complex appears to have a molecular weight of 850,000 daltons. It cross-reacts with human adult haptoglobins. Its electrophoretic mobility was reduced from alpha 2- to beta-globulin when compared with the adult molecule.
摘要
从人类胎儿（妊娠10周）中纯化出了触珠蛋白-血红蛋白复合物。产率为12%，纯化因子约为450。纯化后的复合物分子量似乎为850,000道尔顿。它与成人触珠蛋白发生交叉反应。与成人分子相比，其电泳迁移率从α2球蛋白降低至β球蛋白。
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