对纤维蛋白肽A形成的质子、铜（II）和锌（II）配合物的电位和光谱研究。
A potentiometric and spectroscopic study of the proton, and copper (II) and zinc (II) complexes formed by fibrinopeptide A.
作者信息
Galey J F, Kozlowski H, Pettit L D
机构信息
Laboratoire de Chimie Macromoleculaire, Université des Sciences et Techniques de Lille, France.
出版信息
J Inorg Biochem. 1991 Nov;44(2):149-53. doi: 10.1016/0162-0134(91)84027-7.
Results are reported for a potentiometric and spectroscopic (visible, CD, and EPR) study of the complexes of fibrinopeptide A (Ala-Asp-Ser-Gly-Glu-Gly-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg) with H+, Cu2+ and Zn2+. They show that the peptide forms stable complexes with Cu2+, largely as a result of the Asp2 residue, and that its coordination behavior is almost identical to that of the N-terminal tetrapeptide fragment, Ala-Asp-Ser-Gly. Hence the influence of the remaining amino acid residues on coordination to Cu2+ is insignificant.
报告了对纤维蛋白肽A（丙氨酸-天冬氨酸-丝氨酸-甘氨酸-谷氨酸-甘氨酸-天冬氨酸-苯丙氨酸-亮氨酸-丙氨酸-谷氨酸-甘氨酸-甘氨酸-甘氨酸-缬氨酸-精氨酸）与H⁺、Cu²⁺和Zn²⁺形成的配合物进行电位滴定和光谱（可见光谱、圆二色光谱和电子顺磁共振光谱）研究的结果。结果表明，该肽与Cu²⁺形成稳定的配合物，这主要是由于天冬氨酸2残基的作用，并且其配位行为几乎与N端四肽片段丙氨酸-天冬氨酸-丝氨酸-甘氨酸相同。因此，其余氨基酸残基对与Cu²⁺配位的影响微不足道。
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