血红素与配体蛋白及氨基偶氮染料结合蛋白A的相互作用。
The interactions of haem with ligandin and aminoazo-dye-binding protein A.
作者信息
Tipping E, Ketterer B, Christodoulides L, Enderby G
出版信息
Biochem J. 1976 Aug 1;157(2):461-7. doi: 10.1042/bj1570461.
Abstract
- The interactions of ferriprotoporphyrin IX with ligandin and aminoazo-dye-binding protein A result in absorption spectra in the Soret region characteristic of the ligand in its monomeric state. 2. Both proteins are able to bind ferrous as well as ferric haem. 3. Ferriprotoporphyrin IX is bound at a single site on both proteins. At pH7.0, I 0.16M, difference-spectrophotometric measurements gave association constants of 10(7) and 4 X 10(6) LITRE/MOL FOR LIGANDIN AND PROTEin A respectively. Under the same conditions fluorescence-quenching experiments gave an association constant of 2 X 10(7) litre/mol for ligandin. 4. Bilirubin, bromosulphophthalein and oesterone sulphate each compete with haem for binding by the two proteins. 5. Ferriprotoporphyrin IX bound to both ligandin and protein A is able to form co-ordination complexes with CN-, but not, to any measurable extent, with either N3- or F-. From these results it is suggested that binding by the two proteins may not involve the haem iron atom. 6. Both haem-protein complexes give rise to measurable extrinsic Cotton effects in the Soret region. 7. The formation and properties of the ligandin- and protein A-haem complexes are compared with those of haem-albumin, haemoglobin, myoglobin and other haemoproteins.
摘要
- 高铁原卟啉IX与配体蛋白和氨基偶氮染料结合蛋白A的相互作用，导致在索雷特区域出现单体状态配体特有的吸收光谱。2. 这两种蛋白质都能结合亚铁血红素和高铁血红素。3. 高铁原卟啉IX在这两种蛋白质上的结合位点均为单个。在pH7.0、离子强度0.16M条件下，差示分光光度法测量得出配体蛋白和蛋白A与配体的缔合常数分别为10⁷和4×10⁶升/摩尔。在相同条件下，荧光猝灭实验得出配体蛋白与配体的缔合常数为2×10⁷升/摩尔。4. 胆红素、溴磺酞和硫酸雌酮均与血红素竞争这两种蛋白质的结合位点。5. 与高铁原卟啉IX结合的配体蛋白和蛋白A均能与CN⁻形成配位络合物，但与N₃⁻或F⁻均未形成可测量程度的配位络合物。根据这些结果推测，这两种蛋白质的结合可能不涉及血红素铁原子。6. 两种血红素蛋白复合物在索雷特区域均产生可测量的非固有科顿效应。7. 将配体蛋白和蛋白A - 血红素复合物的形成及性质与血红素 - 白蛋白、血红蛋白、肌红蛋白及其他血红素蛋白的形成及性质进行了比较。
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