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Oxygen equilibrium of hemoglobins containing unnatural hemes. Effect of modification of heme carboxyl groups and side chains at positions 2 and 4.

作者信息

Sugita Y, Yoneyama Y

出版信息

J Biol Chem. 1971 Jan 25;246(2):389-94.

PMID:5542008
Abstract
摘要

相似文献

1
Oxygen equilibrium of hemoglobins containing unnatural hemes. Effect of modification of heme carboxyl groups and side chains at positions 2 and 4.
J Biol Chem. 1971 Jan 25;246(2):389-94.
2
Heme modification studies of myoglobin. I. Purification and some optical and EPR characteristics of synthesized myoglobins containing unnatural hemes.肌红蛋白的血红素修饰研究。I. 含非天然血红素的合成肌红蛋白的纯化及一些光学和电子顺磁共振特性
Biochim Biophys Acta. 1973 Feb 21;295(2):467-79.
3
Nonequivalence of the alpha and beta chains in the oxygen dissociation from hybrid-heme gemoglobin.
J Biol Chem. 1972 Oct 10;247(19):6092-5.
4
Studies on reconstituted myoglobins and hemoglobins. I. Role of the heme side chains in the oxygenation of myoglobin.
J Biochem. 1982 Dec;92(6):1703-12. doi: 10.1093/oxfordjournals.jbchem.a134100.
5
[Circular dichroism study of alkyl isocyanide complexes from heme proteins].[来自血红素蛋白的烷基异腈配合物的圆二色性研究]
Biochim Biophys Acta. 1970 Oct 20;221(1):9-19.
6
Distribution of heme in systems containing heme-free and heme-bound hemoglobin chains.血红素在含有无血红素和血红素结合血红蛋白链的体系中的分布。
Biochemistry. 1971 Sep 28;10(20):3790-5. doi: 10.1021/bi00796a023.
7
Studies on reconstituted myoglobins and hemoglobins. II. Role of the heme side chains in the oxygenation of hemoglobin.重组肌红蛋白和血红蛋白的研究。II. 血红素侧链在血红蛋白氧合作用中的作用。
J Biochem. 1982 Dec;92(6):1713-22. doi: 10.1093/oxfordjournals.jbchem.a134101.
8
Studies on modified hemoglobins. 1. Preparation and properties of a hemoglobin containing heme only in -chains.修饰血红蛋白的研究。1. 仅在β链中含血红素的血红蛋白的制备及性质
Arch Biochem Biophys. 1971 Aug;145(2):448-55. doi: 10.1016/s0003-9861(71)80004-8.
9
Oxygen equilibrium and circular dichroism of hemoglobin-Rainer ( 2 2 1 45Tyr leads to Cys).血红蛋白 - 雷纳(2 2 1 45位酪氨酸突变为半胱氨酸)的氧平衡和圆二色性
J Biol Chem. 1972 Jan 10;247(1):285-90.
10
The reactivity of the tyrosyl residues of cytochrome b 5 .
J Biol Chem. 1972 Jul 25;247(14):4648-53.

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1
Structural origin of cooperativity in human hemoglobin: a view from different roles of α and β subunits in the αβ tetramer.人血红蛋白协同性的结构起源:从αβ四聚体中α和β亚基的不同作用角度看
Biophys Rev. 2022 Apr 18;14(2):483-498. doi: 10.1007/s12551-022-00945-7. eCollection 2022 Apr.
2
Temperature dependent soret spectral band shifts accompany human CN-mesohemoglobin assembly.
Protein J. 2007 Jun;26(4):257-63. doi: 10.1007/s10930-006-9067-7.
3
Bohr-effect and pH-dependence of electron spin resonance spectra of a cobalt-substituted monomeric insect haemoglobin.钴取代的单体昆虫血红蛋白电子自旋共振光谱的玻尔效应和pH依赖性
Biophys Struct Mech. 1982;8(3):189-211. doi: 10.1007/BF00535459.
4
Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins.血红素蛋白中血红素紊乱的质子核磁共振表征
Proc Natl Acad Sci U S A. 1978 Dec;75(12):5755-9. doi: 10.1073/pnas.75.12.5755.
5
Sequence of oxygen binding by hemoglobin.血红蛋白与氧结合的顺序。
Proc Natl Acad Sci U S A. 1978 Nov;75(11):5462-5. doi: 10.1073/pnas.75.11.5462.