Ion Trap Collision-Induced Dissociation of Human Hemoglobin α-Chain Cations

被引：0

作者：

Mekecha, Tegafaw T. ^{[1
]}

Amunugama, Ravi ^{[1
]}

McLuckey, Scott A. ^{[1
]}

机构：

[1] Department of Chemistry, Purdue University, West Lafayette, IN, United States

来源：

Journal of the American Society for Mass Spectrometry | 2006年 / 17卷 / 07期

关键词：

Multiply protonated human hemoglobin α-chain species; ranging from [M + 4H]4+ to [M + 20H]20+; have been subjected to ion trap collisional activation. Cleavages at 88 of the 140 peptide bonds were indicated; summed over all charge states; although most product ion signals were concentrated in a significantly smaller number of channels. Consistent with previous whole protein ion dissociation studies conducted under similar conditions; the structural information inherent to a given precursor ion was highly sensitive to charge state. A strongly dominant cleavage at D75/M76; also noted previously in beam-type collisional activation studies; was observed for the [M + 8H]8+ to [M + 11H]11+ precursor ions. At lower charge states; C-terminal aspartic acid cleavages were also prominent but the most abundant products did not arise from the D75/M76 channel. The [M + 12H]12+-[M + 16H]16+ precursor ions generally yielded the greatest variety of amide bond cleavages. With the exception of the [M + 4H]4+ ion; all charge states showed cleavage at the L113/P114 bond. This cleavage proved to be the most prominent dissociation for charge states [M + 14H]14+ and higher. The diversity of dissociation channels observed within the charge state range studied potentially provides the opportunity to localize residues associated with variants via a top-down tandem mass spectrometry approach. © 2006 American Society for Mass Spectrometry;

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摘要：

Journal article (JA)

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页码：923 / 931