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通过制备性等电聚焦法分离两种单铁人转铁蛋白。

Isolation of the two monoferric human transferrins by preparative isoelectric focussing.

作者信息

van Eijk H G, van Noort W L, Kroos M J, van der Heul C

出版信息

J Clin Chem Clin Biochem. 1980 Sep;18(9):563-6. doi: 10.1515/cclm.1980.18.9.563.

DOI:10.1515/cclm.1980.18.9.563
PMID:7441182
Abstract
  1. Human transferrin was labelled with Fe(III) in nitrilo triacetate buffer at one of its two metal binding sites by variation of the pH. The A-site was preferentially labelled at pH 7.2, the B-site at pH 9.2. 2. The monoferric transferrin preparations were subjected to preparative isoelectric focussing, isolated from the granulated gels, and checked for homogeneity and purity on an analytical scale by isoelectric focussing. 3. The technique for obtaining stable monoferric transferrin (Fe)(A) and transferrin (Fe)(B) preparations is described in detail.
摘要
  1. 通过改变pH值,在氮川三乙酸缓冲液中,人转铁蛋白在其两个金属结合位点之一被Fe(III)标记。在pH 7.2时,A位点优先被标记;在pH 9.2时,B位点优先被标记。2. 将单铁转铁蛋白制剂进行制备性等电聚焦,从颗粒状凝胶中分离出来,并通过等电聚焦在分析规模上检查其均一性和纯度。3. 详细描述了获得稳定的单铁转铁蛋白(Fe)(A)和转铁蛋白(Fe)(B)制剂的技术。

相似文献

1
Isolation of the two monoferric human transferrins by preparative isoelectric focussing.通过制备性等电聚焦法分离两种单铁人转铁蛋白。
J Clin Chem Clin Biochem. 1980 Sep;18(9):563-6. doi: 10.1515/cclm.1980.18.9.563.
2
Analysis of the iron-binding sites of transferrin by isoelectric focussing.通过等电聚焦分析转铁蛋白的铁结合位点。
J Clin Chem Clin Biochem. 1978 Oct;16(10):557-60. doi: 10.1515/cclm.1978.16.10.557.
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No functional difference of the two iron-binding sites of human transferrin in vitro.人转铁蛋白两个铁结合位点在体外无功能差异。
Clin Sci (Lond). 1981 Feb;60(2):185-90. doi: 10.1042/cs0600185.
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In vitro and in vivo studies of iron delivery by human monoferric transferrins.人单铁转铁蛋白铁传递的体外和体内研究
Br J Haematol. 1984 Apr;56(4):571-80. doi: 10.1111/j.1365-2141.1984.tb02182.x.
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Gel isoelectric focusing of human-serum transferrin.人血清转铁蛋白的凝胶等电聚焦
Eur J Biochem. 1976 Sep 15;68(2):333-8. doi: 10.1111/j.1432-1033.1976.tb10819.x.
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Uptake and release of iron from human transferrin.铁从人转铁蛋白中的摄取与释放
Proc Natl Acad Sci U S A. 1981 Apr;78(4):2572-6. doi: 10.1073/pnas.78.4.2572.
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Metalloprotein analysis by capillary isoelectric focusing.通过毛细管等电聚焦进行金属蛋白分析。
J Chromatogr B Biomed Sci Appl. 1997 Mar 7;690(1-2):43-54. doi: 10.1016/s0378-4347(96)00407-0.
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Iron uptake from rat plasma transferrin by rat reticulocytes.大鼠网织红细胞从大鼠血浆转铁蛋白摄取铁。
J Clin Invest. 1978 Nov;62(5):944-51. doi: 10.1172/JCI109223.
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The effect of pH upon human transferrin: selective labelling of the two iron-binding sites.pH对人转铁蛋白的影响:两个铁结合位点的选择性标记
Br J Haematol. 1976 Mar;32(3):341-50. doi: 10.1111/j.1365-2141.1976.tb00937.x.
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Mössbauer studies of electrophoretically purified monoferric and diferric human transferrin.用电泳法纯化的单铁和双铁人转铁蛋白的穆斯堡尔研究
Biol Met. 1988;1(1):26-32. doi: 10.1007/BF01128014.

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Glycoconj J. 1997 Feb;14(2):289-95. doi: 10.1023/a:1018510309524.
2
Uptake and release of iron from human transferrin.铁从人转铁蛋白中的摄取与释放
Proc Natl Acad Sci U S A. 1981 Apr;78(4):2572-6. doi: 10.1073/pnas.78.4.2572.
3
Two-dimensional electrophoresis of cerebrospinal fluid proteins in normal and pathological conditions.正常及病理状态下脑脊液蛋白质的二维电泳
Neurochem Res. 1985 Sep;10(9):1203-19. doi: 10.1007/BF00964840.