含L-组氨酸肽的铜离子配合物的可见光谱和旋光性质 - Suppr

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超能文献

Visible spectra and optical rotatory properties of cupric ion complexes of L-histidine-containing peptides.

作者信息

Bryce G F, Gurd F R

出版信息

J Biol Chem. 1966 Jan 10;241(1):122-9.

PMID:5901043

Abstract

摘要

相似文献

Visible spectra and optical rotatory properties of cupric ion complexes of L-histidine-containing peptides.含L-组氨酸肽的铜离子配合物的可见光谱和旋光性质

J Biol Chem. 1966 Jan 10;241(1):122-9.

Optical rotatory properties of cupric ion complexes of simple dipeptides.简单二肽铜离子络合物的旋光性质

J Biol Chem. 1965 Oct;240(10):3829-36.

Cupric ion complexes of histidine-containing peptides.

J Biol Chem. 1965 Oct;240(10):3837-46.

Optical rotatory dispersion and circular dichroism spectra of copper(II)- and nickel(II)-peptide complexes.铜（II）-和镍（II）-肽配合物的旋光色散和圆二色光谱

J Biol Chem. 1966 Mar 25;241(6):1439-48.

The copper-poly-L-histidine complexes. II. Physicochemical properties.

J Am Chem Soc. 1972 Sep 20;94(19):6844-8. doi: 10.1021/ja00774a044.

High-performance liquid chromatography of preparations of ribonucleic acid inactivator(s) from cupric ion and hydroquinone before and after treatment with histidine.用组氨酸处理前后，来自铜离子和对苯二酚的核糖核酸灭活剂制剂的高效液相色谱分析

J Pharm Sci. 1983 Mar;72(3):300-3. doi: 10.1002/jps.2600720323.

Visible, optical rotatory dispersion, and paramagnetic resonance spectra of the L-histidine--cu(II)--L-threonine complex.L-组氨酸 - 铜（II） - L-苏氨酸配合物的可见光谱、旋光色散光谱和顺磁共振光谱

Can J Biochem. 1968 Jun;46(6):595-600. doi: 10.1139/o68-091.

L-histidine-containing peptides as models for the interaction of copper (II) and nickel (II) ions with sperm whale apomyoglobin.含L-组氨酸的肽作为铜（II）和镍（II）离子与抹香鲸脱辅基肌红蛋白相互作用的模型。

J Biol Chem. 1966 Mar 10;241(5):1072-80.

On the structure of copper(II)-histidine complexes.关于铜（II）-组氨酸配合物的结构

Biochim Biophys Acta. 1970 Feb 17;200(2):411-3. doi: 10.1016/0005-2795(70)90185-6.

Coordination modes of histidine. 4. Coordination structures in the copper(II)-L-histidine (1:2) system.组氨酸的配位模式。4. 铜（II）-L-组氨酸（1:2）体系中的配位结构。

J Inorg Biochem. 1983 Feb;18(1):19-31. doi: 10.1016/0162-0134(83)85036-3.

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