使用质谱技术对由富马酸双（3,5-二溴水杨酸）交联的人血红蛋白进行结构表征。
Structural characterization of human hemoglobin crosslinked by bis(3,5-dibromosalicyl) fumarate using mass spectrometric techniques.
作者信息
Yu Z, Friso G, Miranda J J, Patel M J, Lo-Tseng T, Moore E G, Burlingame A L
机构信息
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446, USA.
出版信息
Protein Sci. 1997 Dec;6(12):2568-77. doi: 10.1002/pro.5560061209.
Diaspirin crosslinked hemoglobin (DCLHb) was analyzed by mass spectrometric-based techniques to identify the protein modifications effected by the crosslinking reaction with bis(3,5-dibromosalicyl) fumarate. DCLHb consists of two principal components. These components were isolated by size-exclusion chromatography and identified by measurement of their molecular weight using electrospray mass spectrometry and subsequent peptide mass mapping and mass spectrometric sequence analysis of their individual digests. Three major RP-HPLC fractions were observed from the major hemoglobin in DCLHb. Their MWs matched the MW of heme, intact hemoglobin beta-chain, and two hemoglobin alpha-chains crosslinked by a fumarate moiety, respectively. The minor HPLC peaks of DCLHb were also separated, and characterized by mass spectrometric methods. These minor components revealed additional details of the structural nature of covalent modification of DCLHb.
采用基于质谱的技术分析双阿司匹林交联血红蛋白（DCLHb），以鉴定与富马酸双（3,5-二溴水杨酸）交联反应所引起的蛋白质修饰。DCLHb由两个主要成分组成。通过尺寸排阻色谱法分离这些成分，并使用电喷雾质谱法测量其分子量，随后对其各自的酶解产物进行肽质量图谱分析和质谱序列分析来鉴定。从DCLHb中的主要血红蛋白观察到三个主要的反相高效液相色谱（RP-HPLC）馏分。它们的分子量分别与血红素、完整血红蛋白β链以及由富马酸部分交联的两条血红蛋白α链的分子量相匹配。DCLHb的次要HPLC峰也被分离出来，并通过质谱方法进行表征。这些次要成分揭示了DCLHb共价修饰结构性质的更多细节。
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