Bresciani D
Biochem J. 1977 May 1;163(2):393-5. doi: 10.1042/bj1630393.
The technique of competitive double-labelling [H. Kaplan, K.J. Stevenson & B.S. Hartley, (1971) Biochem. J. 124, 289-299; L.P. Visentin & H. Kaplan (1975) Biochemistry 14, 463-468] was used to determine the reactivity of some amino groups towards acetic anhydride in deoxy-and liganded haemoglobin. Only those amino groups known to form salt bridges in deoxy-but not in liganded haemoglobin (i.e. the alpha-amino group of valine-1 alpha and the xi-amino group of lysine-40 alpha and lysine-127 alpha [M. F. Perutz (1970) Nature (London) 228, 726-739]) and different reactivities in the two structures.
采用竞争性双标记技术[H. 卡普兰、K.J. 史蒂文森和B.S. 哈特利,(1971年)《生物化学杂志》124卷,289 - 299页;L.P. 维森廷和H. 卡普兰(1975年)《生物化学》14卷,463 - 468页]来测定脱氧血红蛋白和配体血红蛋白中某些氨基与乙酸酐的反应活性。只有那些已知在脱氧血红蛋白中形成盐桥而在配体血红蛋白中不形成盐桥的氨基(即缬氨酸-1α的α-氨基以及赖氨酸-40α和赖氨酸-127α的ξ-氨基[M.F. 佩鲁茨(1970年)《自然》(伦敦)228卷,726 - 739页]),并且在两种结构中具有不同的反应活性。