Acid-base titration of hemocyanin from Octopus vulgaris Lam.
Acid-base titration of hemocyanin from Octopus vulgaris Lam.
复制标题
章鱼血蓝蛋白的酸碱滴定。
DOI：
10.1021/bi00720a015
复制
发表时间：
1974
期刊：
影响因子：
2.9
通讯作者：
F. Ghiretti
中科院分区：
文献类型：
--
作者：
B. Salvato;A. Ghiretti;F. Ghiretti
电位滴定法和分光光度滴定法-通过滴定天然（含氧和脱氧）和铜来确定这些基团是组氨酸-在平衡状态下，在3 M尿素和0.5 M胍的存在下，在10,25和几个实验条件下进行了章鱼游离血青素中的天然和无铜蛋白质。酸- 30的结果。在KC1溶液中，用分光光度法对天然碱和伪碱进行连续滴定，在25℃下，在不同的KC1 - mocyanin中，以及在尿素和胍中，硫离子强度表明，尿素和硫氰酸盐中的两种铜均显示出，氧、铜和功能亚基（50.800）上的原子与其他四个配体结合，在强疏水环境中对构象非羧基有很强的稳定作用。蛋白质的形成。
Potentiometric and spectrophotometric titra- These groups have been identified as histidines by titrating tions of native (oxygenated and deoxygenated) and copper- at equilibrium the native and copper-free proteins in the free hemocyanin of Octopus vulgaris have been carried out presence of 3 M urea and 0.5 M guanidine at 10, 25, and under several experimental conditions. The results of acid- 30. The spectrophotometric titration of native and apohe-base continuous titration at 25 in KC1 solutions at differ- mocyanin in KC1, as well as in urea and guanidine, thio-ent ionic strengths indicate that each of the two copper urea, and thiocyanate, has shown that oxygen, copper, and atoms in the functional subunit (50.800) is bound to four otherligands have a strong stabilizing effect on the confornon-carboxyl groups in a strong hydrophobic environment. mation of the protein.