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The effect of iron binding on the conformation of transferrin. A small angle x-ray scattering study.铁结合对转铁蛋白构象的影响。小角X射线散射研究。
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本文引用的文献

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Physical characteristics of human transferrin from small angle neutron scattering.小角中子散射法测定人转铁蛋白的物理特性
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2
Characterization of transferrin metal-binding sites by diffusion-enhanced energy transfer.通过扩散增强能量转移对转铁蛋白金属结合位点进行表征。
Biochemistry. 1980 Oct 28;19(22):5057-62. doi: 10.1021/bi00563a019.
3
Size and shape determination of apotransferrin and transferrin monomers.
Biopolymers. 1971 Jun;10(6):1039-48. doi: 10.1002/bip.360100610.
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The reaction of ferric salts with transferrin.铁盐与转铁蛋白的反应。
J Biol Chem. 1973 May 10;248(9):3228-32.
5
Studies on the active center of pancreatic amylase. II. Small angle x-ray scattering investigations.胰腺淀粉酶活性中心的研究。II. 小角X射线散射研究。
Mol Cell Biochem. 1974 Oct 30;4(3):211-6. doi: 10.1007/BF01731483.
6
Study of the position of NAD and its effect on the conformation of D-glyceraldehyde-3-phosphate dehydrogenase by small-angle x-ray scattering.通过小角X射线散射研究NAD的位置及其对3-磷酸甘油醛脱氢酶构象的影响。
Eur J Biochem. 1972 Oct 17;30(1):184-9. doi: 10.1111/j.1432-1033.1972.tb02085.x.
7
Conformation of human IgG subclasses in solution. Small-angle X-ray scattering and hydrodynamic studies.溶液中人类免疫球蛋白G亚类的构象。小角X射线散射和流体动力学研究。
Eur J Biochem. 1985 Feb 15;147(1):17-25. doi: 10.1111/j.1432-1033.1985.tb08712.x.
8
The detection of four molecular forms of human transferrin during the iron binding process.铁结合过程中人类转铁蛋白四种分子形式的检测
Biochim Biophys Acta. 1976 Nov 26;453(1):250-6. doi: 10.1016/0005-2795(76)90270-1.
9
The effect of trypsin on bovine transferrin and lactoferrin.胰蛋白酶对牛转铁蛋白和乳铁蛋白的作用。
Biochim Biophys Acta. 1976 Sep 28;446(1):214-25. doi: 10.1016/0005-2795(76)90112-4.
10
Preliminary x-ray study of crystals of human transferrin.人转铁蛋白晶体的初步X射线研究。
J Mol Biol. 1978 Aug 5;123(2):285-6. doi: 10.1016/0022-2836(78)90328-5.

铁结合对转铁蛋白构象的影响。小角X射线散射研究。

The effect of iron binding on the conformation of transferrin. A small angle x-ray scattering study.

作者信息

Kilár F, Simon I

出版信息

Biophys J. 1985 Nov;48(5):799-802. doi: 10.1016/S0006-3495(85)83838-8.

DOI:10.1016/S0006-3495(85)83838-8
PMID:4074838
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1329405/
Abstract

Distance distribution functions, p(r), radii of gyration, Rg, and radii of gyration of cross section, Rq, of apotransferrin, monoferric transferrin, and diferric transferrin have been compared. The alteration of Rg and Rq upon iron binding has been determined by a difference method. An unusual feature of the stepwise structural changes of transferrin upon iron saturation is that binding of the first ferric ion is responsible for more than half of the whole change in Rq, whereas Rg alters significantly only after the binding of the second ferric ion.

摘要

已对脱铁转铁蛋白、单铁转铁蛋白和双铁转铁蛋白的距离分布函数p(r)、回转半径Rg以及横截面回转半径Rq进行了比较。通过差值法确定了铁结合后Rg和Rq的变化。转铁蛋白在铁饱和时逐步发生结构变化的一个不寻常特征是,第一个铁离子的结合导致了Rq整体变化的一半以上,而Rg仅在第二个铁离子结合后才发生显著变化。