共查询到17条相似文献,搜索用时 203 毫秒
1.
2.
3.
猪脾铁蛋白电子隧道特性及释放铁途径的研究 总被引:13,自引:0,他引:13
维生素C和连二亚硫酸钠混合后只能加速猪脾铁蛋白释放铁的速率,并不能使铁蛋白释放铁的动力学途径由复杂转化为简单.而单独维生素C却能利用蛋白壳上的电子隧道传递电子,迫使铁蛋白以二分之一的反应级数方式释放整体铁核的铁并起着抗磷酸盐阻遏释放铁速率的作用,简化释放铁的途径.对维生素C参与铁蛋白释放铁的机理进行了讨论. 相似文献
4.
棕色固氮菌细菌铁蛋白释放铁的动力学方程和性质 总被引:2,自引:0,他引:2
棕色固氮菌细菌铁蛋白铁核中的磷铁组成存在非均匀性。细菌铁蛋白释放铁的动力学特性表现出复杂性。通过动力学曲线分析,提出蛋白壳自身调节能力起着限制释放铁速率关键步骤的观点,建立分析铁蛋白释放铁的动力学特性方程并用它较合理地阐明铁蛋白释放铁的动力学规律及储存铁的途径。用分光光度法和动力学方程研究细菌铁蛋白释放铁的全过程,其结果表明该蛋白以一级反应方式释放铁核表层的铁和以零级反应方式释放铁核内层的铁。外加磷酸盐能强烈地抑制释放铁的速率,引起释放铁的反应级数的转化,迫使铁蛋白以一级反应的方式释放铁核中的大多数铁。 相似文献
5.
棕色固氮菌细菌铁蛋白释放铁的动力学方程和性质 总被引:2,自引:1,他引:1
棕色固氮菌细胞铁蛋白铁核中的磷铁组成存在非均匀性。细菌铁蛋白释放铁的动力学特性表现出复杂性。通过动力学曲线分析,提出蛋白壳自身调节能力起着限制释放铁速率关键步骤的观点建立分析铁蛋白释放铁的动力学特性方程并用它较合理地阐明铁蛋白释放铁的动力不储存铁的途径。用分光光度法和动力学方程研究细胞铁蛋白释放铁的全过程。其表明该蛋白以一级反应方式释放铁核表层的铁和以零级反应方式释放铁核内层的铁。外加磷酸盐能强烈 相似文献
6.
分别制备含有魟鱼肝铁蛋白(1iver ferritin of Dasyatis akajei,DALF)和海兔肝铁蛋白(Liver ferritin of Aplysia,ALF)的混合蛋白质体系。选用电子光谱技术和不同电子供体,研究在混合蛋白质体系中,DALF和ALF释放铁的动力学过程和规律。实验结果表明,采用Na2S2O4作为还原剂时,DALF以两相行为进行释放铁的反应;而选用抗坏血酸作为还原剂时,DALF却以一级反应动力学方式进行释放铁的反应,简化释放铁的过程。在混合蛋白质体系中且以抗坏血酸和Na2S2O4为电子供体时,ALF均以一级反应动力学过程进行释放铁的反应,认为某些蛋白质参与协助ALF释放铁反应,从而简化释放铁的过程。 相似文献
7.
比较了天然和人工重合成铁核的马脾铁蛋白以及模拟化合物的穆斯堡尔谱,由此探讨了铁蛋白分子内腔铁核的结构和形成机制。结果表明:它们的穆斯堡尔谱和各参数值均很接近。 相似文献
8.
比较了天然和人工重合成铁核的马脾铁蛋白以及模拟化合物的穆斯堡尔谱,由此探讨了铁蛋白分子内腔铁核的结构和形成机制。结果表明:它们的穆斯堡尔谱和各参数值均很接近。 相似文献
9.
10.
11.
Arsenic species that cause release of iron from ferritin and generation of activated oxygen 总被引:9,自引:0,他引:9
The in vitro effects of four different species of arsenic (arsenate, arsenite, monomethylarsonic acid, and dimethylarsinic acid) in mobilizing iron from horse spleen ferritin under aerobic and anaerobic conditions were investigated. Dimethylarsinic acid (DMA(V)) and dimethylarsinous acid (DMA(III)) significantly released iron from horse spleen ferritin either with or without the presence of ascorbic acid, a strong synergistic agent. Ascorbic acid-mediated iron release was time-dependent as well as both DMA(III) and ferritin concentration-dependent. Iron release from ferritin by DMA(III)) alone or with ascorbic acid was not significantly inhibited by superoxide dismutase (150 or 300 units/ml). However, the iron release was greater under anaerobic conditions (nitrogen gas), which indicates direct chemical reduction of iron from ferritin by DMA(III), with or without ascorbic acid. Both DMA(V) and DMA(III)) released iron from both horse spleen and human liver ferritin. Further, the release of ferritin iron by DMA(III)) with ascorbic acid catalyzed bleomycin-dependent degradation of calf thymus DNA. These results indicate that exogenous methylated arsenic species and endogenous ascorbic acid can cause (a) the release of iron from ferritin, (b) the iron-dependent formation of reactive oxygen species, and (c) DNA damage. This reactive oxygen species pathway could be a mechanism of action of arsenic carcinogenesis in man. 相似文献
12.
Kinetics of iron release from pig spleen ferritin with bare platinum electrode reduction 总被引:3,自引:0,他引:3
Several anaerobic electrochemical cells were employed to study the kinetics of iron release from pig spleen ferritin (PSF) at a bare platinum electrode. Controlled potential microcoulometry (CPM) is the principal technology used to investigate the kinetics in the absence of a mediator. A kinetic study of iron release by microcoulometry has revealed that ferritin undergoes direct electron transfer at the electrode in the absence of a mediator, indicating that ferritin is an electroactive protein. Several experiments failed to show that alpha'alpha-bipyridyl has the capacity to reduce hydrolyzed Fe(3+) within the ferritin core after it has been reduced by the electrode at -600 mV vs. NHE in the absence of mediator. PSF is known to bind heme to generate a hemeoprotein, named pig spleen hemeoferritin (PSF(ho)). The rate of iron release is accelerated by the heme binding to PSF(ho) without the need for small mediators. Under similar conditions, two kinetic processes for iron release from PSF and bacterial ferritin of Azoaobacter vinelandii (AvBF) were studied and both fit a zero-order law. In addition, the rate of iron release in PSF can be accelerated two-fold by a specific reduction system consisting of ascorbic acid (AA) and the bare platinum electrode at -600 mV. However, this kinetic process does not follow zero-, half-, first, or second-order rate laws. A model is proposed to explain a mechanism of direct electron transfer between ferritin and the electrode is derived to describe the kinetics of iron release. 相似文献
13.
The extended X-ray absorption fine structure (EXAFS) associated with the iron K-edge has been measured and interpreted for ferritin and haemosiderin extracted from horse spleen, and haemosiderin extracted from the livers of humans with treated primary haemochromatosis, and from the spleens of humans with treated secondary haemochromatosis. For ferritin, the data are consistent with, on average, each iron atom being in an environment comprised of approx. six oxygen atoms at 1.93 +/- 0.02 A, approx. 1.5 iron atoms at 2.95 +/- 0.02 A and approx. 1.1 iron atoms at 3.39 +/- 0.02 A, with a further shell of oxygens at approx. 3.6 A. Iron in horse spleen haemosiderin is in an essentially identical local environment to that in horse spleen ferritin. In contrast, the EXAFS data for primary haemochromatosis haemosiderin indicate that the iron-oxide core is amorphous; only a single shell of approx. six oxygen atoms at approx. 1.94 +/- 0.02 A being apparent. Secondary haemochromatosis haemosiderin shows an ordered structure with approx. 1.4 iron atoms at both 2.97 +/- 0.02 and 3.34 +/- 0.02 A. This arrangement of iron atoms is similar to that in horse spleen haemosiderin, but the first oxygen shell is split with approx. 2.9 atoms at 1.90 +/- 0.02 A and approx. 2.7 at 2.03 +/- 0.02 A, indicative of substantial structural differences between secondary haemochromatosis haemosiderin and horse spleen haemosiderin. 相似文献
14.
R.J. Ulvik I. Romslo F. Roland R.R. Crichton 《Biochimica et Biophysica Acta (BBA)/General Subjects》1981,677(1):50-56
Mitochondria mobilize iron from ferritin by a mechanism that depends on external FMN. With rat liver mitochondria, the rate of mobilization of iron is higher from rat liver ferritin than from horse spleen ferritin. With horse liver mitochondria, the rate of iron mobilization is higher from horse spleen ferritin than from rat liver ferritin. The results are explained by a higher affinity between mitochondria and ferritins of the same species. The mobilization of iron increases with the iron content of the ferritin and then levels off. A maximum is reached with ferritins containing about 1 200 iron atoms per molecule. The results represent further evidence that ferritin may function as a direct iron donor to the mitochondria. 相似文献
15.
Dynamic equilibria in iron uptake and release by ferritin 总被引:7,自引:0,他引:7
The function of ferritins is to store and release ferrous iron. During oxidative iron uptake, ferritin tends to lower Fe2+ concentration, thus competing with Fenton reactions and limiting hydroxy radical generation. When ferritin functions as a releasing iron agent, the oxidative damage is stimulated. The antioxidant versus pro-oxidant functions of ferritin are studied here in the presence of Fe2+, oxygen and reducing agents. The Fe2+-dependent radical damage is measured using supercoiled DNA as a target molecule. The relaxation of supercoiled DNA is quantitatively correlated to the concentration of exogenous Fe2+, providing an indirect assay for free Fe2+. After addition of ferrous iron to ferritin, Fe2+ is actively taken up and asymptotically reaches a stable concentration of 1–5
m. Comparable equilibrium concentrations are found with plant or horse spleen ferritins, or their apoferritins. After addition of ascorbate, iron release is observed using ferrozine as an iron scavenger. Rates of iron release are dependent on ascorbate concentration. They are about 10 times larger with pea ferritin than with horse ferritin. In the absence of ferrozine, the reaction of ascorbate with ferritins produces a wave of radical damage; its amplitude increases with increased ascorbate concentrations with plant ferritin; the damage is weaker with horse ferritin and less dependent on ascorbate concentrations. 相似文献
16.
Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones 总被引:19,自引:0,他引:19
D Boyd C Vecoli D M Belcher S K Jain J W Drysdale 《The Journal of biological chemistry》1985,260(21):11755-11761
We have isolated essentially full-length cDNA clones for human ferritin H and L chains from a human liver cDNA library. This allows the first comparison of H and L nucleotide and amino acid sequences from the same species as well as ferritin L cDNA sequences from different species. We conclude that human H and L ferritins are related proteins which diverged about the time of evolution of birds and mammals. We also deduce the secondary structure of the H and L subunits and compare this with the known structure of horse spleen ferritin. We find that residues involved in subunit interaction in shell assembly are highly conserved in H and L sequences. However, we find several interesting differences in H subunits at the amino acid residues involved in iron transport and deposition. These substitutions could account for known differences in the uptake, storage, and release of iron from isoferritins of different subunit composition. 相似文献
17.
Ferritins are a class of iron storage protein spheres found mainly in the liver and spleen, which have attracted many research interests due to their unique structural features and biological properties. Recently, ferritin and apoferritin (ferritin devoid of the iron core), have been employed as chemically addressable nanoscale building blocks for functional materials development. However, the reactive residues of apoferritin or ferritin have never been specified and it is still unclear about the chemoselectivity of apoferritin towards different kinds of bioconjugation reagents. In this work, matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry combined with enzymatic digestion analysis was used to identify the reactive lysine residues of horse spleen apoferritin when conjugated with N-hydroxysuccinimide reagents. The result demonstrated that among all the lysine residues, K97, K83, K104, K67 and K143 are the reactive ones that can be addressed. 相似文献