Brennan S O, Jones K O, Crethar L, Arnold B J, Fleming P J, Winterbourn C C
Biochim Biophys Acta. 1977 Oct 26;494(2):403-7. doi: 10.1016/0005-2795(77)90169-6.
A new mildly unstable haemoglobin, Hb North Shore (beta134 Val replaced by Glu) is described. It was found in a 4th generation Australian of Anglo-Celtic origin with a mild microcytic anaemia. The charge change involved is partially obscured as evidenced by the electrophoretic mobility of the native haemoglobin. The structural studies illustrate the usefulness of Staphylococcus aureus strain V8 protease as a specific cleavage enzyme at glutamyl residues.
本文描述了一种新的轻度不稳定血红蛋白——北岸血红蛋白(Hb North Shore,β134位缬氨酸被谷氨酸取代)。该血红蛋白是在一名具有盎格鲁 - 凯尔特血统的第四代澳大利亚人身上发现的,此人患有轻度小细胞贫血。正如天然血红蛋白的电泳迁移率所证明的那样,所涉及的电荷变化部分被掩盖。结构研究表明,金黄色葡萄球菌V8蛋白酶作为一种在谷氨酰残基处的特异性切割酶具有实用性。