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吡哆醛化合物作为血红蛋白α和β N端的特异性试剂。

Pyridoxal compounds as specific reagents for the alpha and beta N-termini of hemoglobin.

作者信息

Benesch R E, Yung S, Suzuki T, Bauer C, Benesch R

出版信息

Proc Natl Acad Sci U S A. 1973 Sep;70(9):2595-9. doi: 10.1073/pnas.70.9.2595.

Abstract

Bifunctional pyridoxal derivatives with a charged side chain in the 5' position react specifically with the N-terminal valine residues of hemoglobin. Three of these compounds, which have only a single negative charge in the side chain, are highly selective for the alpha-chain N-terminal residues in the oxy conformation while pyridoxal phosphate, with two negative charges, reacts specifically with the beta N-terminal in deoxyhemoglobin. Schiff's base formation, therefore, results in decreased oxygen affinity with pyridoxal phosphate but increased oxygen affinity with the other three compounds. Reduction with sodium borohydride leads to irreversible coupling at either end of the molecule, and preparation and properties of such derivatives are described.

摘要

在5'位置带有带电侧链的双功能吡哆醛衍生物能与血红蛋白的N端缬氨酸残基发生特异性反应。其中三种化合物在侧链上仅带有一个负电荷,对氧合构象中的α链N端残基具有高度选择性,而带有两个负电荷的磷酸吡哆醛则与脱氧血红蛋白中的β N端发生特异性反应。因此,席夫碱的形成导致磷酸吡哆醛使氧亲和力降低,而其他三种化合物则使氧亲和力增加。用硼氢化钠还原会导致分子两端发生不可逆偶联,并描述了此类衍生物的制备方法和性质。

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Bis-pyridoxal polyphosphates: a new class of specific intramolecular crosslinking agents for hemoglobin.
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The Bohr effect of pyridoxylated hemoglobins.吡哆醛化血红蛋白的玻尔效应。
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本文引用的文献

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ON THE DISSOCIATION OF NORMAL ADULT HUMAN HEMOGLOBIN.关于正常成人血红蛋白的解离
Proc Natl Acad Sci U S A. 1963 Oct;50(4):774-82. doi: 10.1073/pnas.50.4.774.
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The removal of organic phosphates from hemoglobin.从血红蛋白中去除有机磷酸盐。
Arch Biochem Biophys. 1971 Jul;145(1):236-9. doi: 10.1016/0003-9861(71)90031-2.

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