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Mechanism for the increase in solubility of deoxyhemoglobin S due to cross-linking the beta chains between lysine-82 beta 1 and lysine-82 beta 2.

作者信息

Chatterjee R, Walder R Y, Arnone A, Walder J A

出版信息

Biochemistry. 1982 Nov 9;21(23):5901-9. doi: 10.1021/bi00266a027.

DOI:10.1021/bi00266a027
PMID:6817783
Abstract
摘要

相似文献

1
Mechanism for the increase in solubility of deoxyhemoglobin S due to cross-linking the beta chains between lysine-82 beta 1 and lysine-82 beta 2.通过赖氨酸-82β1和赖氨酸-82β2之间的β链交联增加脱氧血红蛋白S溶解度的机制。
Biochemistry. 1982 Nov 9;21(23):5901-9. doi: 10.1021/bi00266a027.
2
Structural features required for the reactivity and intracellular transport of bis(3,5-dibromosalicyl)fumarate and related anti-sickling compounds that modify hemoglobin S at the 2,3-diphosphoglycerate binding site.双（3,5 - 二溴水杨酸基）富马酸酯及相关抗镰状化化合物在2,3 - 二磷酸甘油酸结合位点修饰血红蛋白S时的反应性和细胞内转运所需的结构特征。
J Biol Chem. 1984 Dec 10;259(23):14863-73.
3
The effect of 2,3-diphosphoglycerate on the solubility of deoxyhemoglobin S.
Arch Biochem Biophys. 1986 Sep;249(2):301-5. doi: 10.1016/0003-9861(86)90006-8.
4
Ionic strength dependence of the polymer solubilities of deoxyhemoglobin S + C and S + A mixtures.脱氧血红蛋白S+C和S+A混合物聚合物溶解度的离子强度依赖性。
Blood. 1986 Apr;67(4):887-92.
5
Refined crystal structure of deoxyhemoglobin S. I. Restrained least-squares refinement at 3.0-A resolution.脱氧血红蛋白S的精细晶体结构。I. 3.0埃分辨率下的约束最小二乘精修。
J Biol Chem. 1985 Jul 15;260(14):8272-9. doi: 10.2210/pdb1hbs/pdb.
6
Effect of cross-linking between 82 beta 1 and 82 beta 2 lysyl residues on the kinetics of polymerization of deoxyhemoglobin S.82β1和82β2赖氨酰残基之间的交联对脱氧血红蛋白S聚合动力学的影响。
J Biol Chem. 1982 Jul 10;257(13):7525-30.
7
Development of antisickling compounds that chemically modify hemoglobin S specifically within the 2,3-diphosphoglycerate binding site.
J Mol Biol. 1980 Aug 5;141(2):195-216. doi: 10.1016/0022-2836(80)90385-x.
8
Isolation and characterization of a new hemoglobin derivative cross-linked between the alpha chains (lysine 99 alpha 1----lysine 99 alpha 2).
J Biol Chem. 1986 Jul 25;261(21):9929-37.
9
Affinity labeling of hemoglobin with 4,4'-diisothiocyanostilbene-2,2'-disulfonate: covalent cross-linking in the 2,3-diphosphoglycerate binding site.血红蛋白与4,4'-二异硫氰酸芪-2,2'-二磺酸盐的亲和标记：2,3-二磷酸甘油酸结合位点的共价交联
Biochemistry. 1988 Mar 8;27(5):1804-8. doi: 10.1021/bi00405a062.
10
Preparation of intramolecularly cross-linked hemoglobins.
Methods Enzymol. 1994;231:274-80. doi: 10.1016/0076-6879(94)31019-x.

引用本文的文献

1
Haptoglobin preferentially binds β but not α subunits cross-linked hemoglobin tetramers with minimal effects on ligand and redox reactions.触珠蛋白优先结合β亚基而不是α亚基交联的血红蛋白四聚体，对配体和氧化还原反应的影响最小。
PLoS One. 2013;8(3):e59841. doi: 10.1371/journal.pone.0059841. Epub 2013 Mar 29.
2
Combining the influence of two low O2 affinity-inducing chemical modifications of the central cavity of hemoglobin.结合血红蛋白中心腔两个低氧亲和力诱导化学修饰的影响。
Biochemistry. 2007 Apr 17;46(15):4554-64. doi: 10.1021/bi0621462. Epub 2007 Mar 24.
3
Perturbation of the intermolecular contact regions (molecular surface) of hemoglobin S by intramolecular low-O2-affinity-inducing central cavity cross-bridges.
通过分子内低氧亲和力诱导中心腔交叉桥对血红蛋白S分子间接触区域（分子表面）的扰动。
J Protein Chem. 2000 May;19(4):255-67. doi: 10.1023/a:1007039111556.
4
Pro-oxidant effects of cross-linked haemoglobins explored using liposome and cytochrome c oxidase vesicle model membranes.利用脂质体和细胞色素c氧化酶囊泡模型膜探究交联血红蛋白的促氧化作用。
Biochem J. 1995 Sep 15;310 ( Pt 3)(Pt 3):827-33. doi: 10.1042/bj3100827.
5
Preparation, properties, and plasma retention of human hemoglobin derivatives: comparison of uncrosslinked carboxymethylated hemoglobin with crosslinked tetrameric hemoglobin.人血红蛋白衍生物的制备、性质及血浆滞留情况：未交联羧甲基化血红蛋白与交联四聚体血红蛋白的比较
Proc Natl Acad Sci U S A. 1991 Apr 15;88(8):3329-33. doi: 10.1073/pnas.88.8.3329.
6
X-ray diffraction study of the binding of the antisickling agent 12C79 to human hemoglobin.抗镰状化剂12C79与人血红蛋白结合的X射线衍射研究。
Proc Natl Acad Sci U S A. 1991 Mar 15;88(6):2209-11. doi: 10.1073/pnas.88.6.2209.
7
The functional, oxygen-linked chloride binding sites of hemoglobin are contiguous within a channel in the central cavity.血红蛋白的功能性氧连接氯结合位点在中央腔的一个通道内相邻。
J Protein Chem. 1992 Apr;11(2):177-85. doi: 10.1007/BF01025223.