Charge dependence of protonated insulin decompositions

被引:84
作者
Wells, JM
Stephenson, JL
McLuckey, SA [1 ]
机构
[1] Purdue Univ, Dept Chem, Brown Lab 1393, W Lafayette, IN 47907 USA
[2] Oak Ridge Natl Lab, Div Chem & Analyt Sci, Oak Ridge, TN 37831 USA
基金
美国国家卫生研究院;
关键词
insulin; electrospray ionization; unimolecular dissociation; ion/ion reaction; quadrupole ion trap;
D O I
10.1016/S1387-3806(00)00389-4
中图分类号
O64 [物理化学(理论化学)、化学物理学]; O56 [分子物理学、原子物理学];
学科分类号
070203 ; 070304 ; 081704 ; 1406 ;
摘要
Ion trap collisional activation is used to study the effects of charge state on protonated insulin decompositions for three forms of insulin: bovine, porcine, and human. Tandem mass spectrometry data are presented for ions with one to five protons dissociated under identical resonance excitation conditions. The (M+5H)(5+) and (M+4H)(4+) ions fragment exclusively by peptide bond cleavage of bonds outside the cycles formed by the disulfide linkages present in the insulin molecule, whereas the (M+3H)(3+) and (M+2H)(2+) ions appear to show a mixture of peptide bond cleavage and fragments arising from mechanisms associated with disulfide bond cleavage. The (M+H)(+) ion fragments almost exclusively by way of disulfide bond cleavage, with the only major exception being cleavage on the C-terminal side of glutamic acid residues external to the cycles formed by the disulfide linkages. (C) 2000 Elsevier Science B.V.
引用
收藏
页码:A1 / A9
页数:9
相关论文
共 38 条
[1]   CHARACTERIZATION OF DISULFIDE BOND POSITION IN PROTEINS AND SEQUENCE-ANALYSIS OF CYSTINE-BRIDGED PEPTIDES BY TANDEM MASS-SPECTROMETRY [J].
BEAN, MF ;
CARR, SA .
ANALYTICAL BIOCHEMISTRY, 1992, 201 (02) :216-226
[2]   AMINO-ACID SEQUENCING OF PROTEINS [J].
BIEMANN, K ;
PAPAYANNOPOULOS, IA .
ACCOUNTS OF CHEMICAL RESEARCH, 1994, 27 (11) :370-378
[3]   MASS-SPECTROMETRIC DETERMINATION OF THE AMINO-ACID-SEQUENCE OF PEPTIDES AND PROTEINS [J].
BIEMANN, K ;
MARTIN, SA .
MASS SPECTROMETRY REVIEWS, 1987, 6 (01) :1-75
[4]   ACTIVATION-ENERGIES FOR GAS-PHASE DISSOCIATIONS OF MULTIPLY CHARGED IONS FROM ELECTROSPRAY IONIZATION MASS-SPECTROMETRY [J].
BUSMAN, M ;
ROCKWOOD, AL ;
SMITH, RD .
JOURNAL OF PHYSICAL CHEMISTRY, 1992, 96 (06) :2397-2400
[5]   Influence of peptide composition, gas-phase basicity, and chemical modification on fragmentation efficiency: Evidence for the mobile proton model [J].
Dongre, AR ;
Jones, JL ;
Somogyi, A ;
Wysocki, VH .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (35) :8365-8374
[6]   Evolution of ion internal energy during collisional excitation in the Paul ion trap: A stochastic approach [J].
Goeringer, DE ;
McLuckey, SA .
JOURNAL OF CHEMICAL PHYSICS, 1996, 104 (06) :2214-2221
[7]  
Gorman JJ, 1996, RAPID COMMUN MASS SP, V10, P529, DOI 10.1002/(SICI)1097-0231(19960331)10:5<529::AID-RCM522>3.0.CO
[8]  
2-9
[9]   ELECTROSPRAY IONIZATION WITH FOURIER-TRANSFORM MASS-SPECTROMETRY - CHARGE STATE ASSIGNMENT FROM RESOLVED ISOTOPIC PEAKS [J].
HENRY, KD ;
MCLAFFERTY, FW .
ORGANIC MASS SPECTROMETRY, 1990, 25 (09) :490-492
[10]   Determination of disulfide bonds in highly bridged disulfide-linked peptides by matrix-assisted laser desorption/ionization mass spectrometry with postsource decay [J].
Jones, MD ;
Patterson, SD ;
Lu, HS .
ANALYTICAL CHEMISTRY, 1998, 70 (01) :136-143