Characterization of the metal-binding site of human prolactin by site-specific metal-catalyzed oxidation

被引：12
|
作者：
Sadineni, Vikram
Galeva, Nadezhda A.
Schoneich, Christian [1 ]
机构：
[1] Univ Kansas, Dept Pharmaceut Chem, Lawrence, KS 66047 USA
[2] Univ Kansas, Mass Spectrometry Lab, Lawrence, KS 66045 USA
来源：
ANALYTICAL BIOCHEMISTRY | 2006年 / 358卷 / 02期
关键词：
protein; metal-catalyzed oxidation; mass spectrometry; prolactin; metal-binding;
D O I：
10.1016/j.ab.2006.08.026
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Site-specific metal-catalyzed oxidation (MCO) was applied to characterize the metal-binding site (MBS) of recombinant human prolactin (hPRL), which belongs to the hematopoietic cytokine family. Copper and ascorbate of various concentrations were used to initiate the oxidation of hPRL, and the oxidation- sensitive motifs were characterized and quantitated by mass spectrometry. Based on the results obtained with 10 mu M Cu2+ and 0.3-2.0 mM ascorbate, we propose that the MBS in hPRL is composed of His27, His30, and Hisl 73. This result shows the similarity of hPRL to human growth hormone (hGH), a member of the same family as hPRL, where the NIBS is composed of His18, His21, and Glu174. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码：208 / 215
页数：8
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