Plasma desorption mass spectrometry of haemoglobin tryptic peptides for the characterization of a Hungarian α-chain variant

Jensen, Ole Nørregaard; Roepstorff, Peter; Rozynov, B. V.; Horányi, Margit; Szelényi, J.; Hollán, Susan R.; Асеева, Е. А.; Spivak, V.A.

doi:10.1002/bms.1200201002

Cited by 12 publications

(11 citation statements)

References 27 publications

(1 reference statement)

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“…Several groups have identified the a-and b-chain hemoglobin variants using traditional analytical methods 15 and various mass spectrometry techniques, including field desorption, 16 plasma desorption 17 and electrospray. [18][19][20] However, very little attention has been paid to the interactions of hemoglobin with chemotherapeutic drugs, such as cisplatin.…”

Section: Introductionmentioning

confidence: 99%

Studies of cisplatin and hemoglobin interactions using nanospray mass spectrometry and liquid chromatography with inductively-coupled plasma mass spectrometry

Mandal

Teixeira

2003

Analyst

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Interactions of cisplatin with hemoglobin (Hb) were studied using both nanoelectrospray mass spectrometry (nanoESI-MS) and a combination of size exclusion high performance liquid chromatography with inductively coupled plasma mass spectrometry (HPLC-ICPMS). Size exclusion HPLC separation of free and protein-bound cisplatin followed by simultaneous monitoring of 195Pt and 57Fe demonstrated the presence of Hb-bound Pt complexes. Nanospray quadrupole time-of-flight mass spectrometry studies of the Hb-cisplatin complexes further demonstrated the specific binding of cisplatin to the alpha-chain, heme-alpha, beta-chain, and heme-beta units of hemoglobin. Accurate mass measurements and tandem mass spectrometry information confirmed the Hb-cisplatin complexes. The formation of Hb-cisplatin complexes was observed at the sub-microM to microM concentration levels of cisplatin, which are relevant to clinical levels. These findings and the techniques developed for cisplatin-Hb interaction studies are useful for understanding of drug-protein interactions.

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Section: Introductionmentioning

confidence: 99%

Studies of cisplatin and hemoglobin interactions using nanospray mass spectrometry and liquid chromatography with inductively-coupled plasma mass spectrometry

Mandal

Teixeira

2003

Analyst

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“…13 Later, analysis by plasma desorption (PD) was demonstrated to be similarly effective. 17 More recently, electrospray ionization (ESI) mass spectrometry has been applied to the analysis of abnormal hemoglobins. 3,7,9,[18][19][20][21] Using this method, intact globins could be screened for the first time with 0.01% mass accuracy.…”

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confidence: 99%

Rapid Analysis of Hemoglobin from Whole Human Blood by Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry

Houston

Reilly

1997

Rapid Commun. Mass Spectrom.

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Matrix-assisted laser desorption time-of-flight mass spectrometry (MALDI-TOFMS) is applied to the analysis of whole human blood. No separation or purification steps are required to observe individual globins and the sensitivity of the method is excellent. Mass accuracy and precision are 0.01% using a linear TOF system with pulsed ion extraction. Sickle-cell hemoglobin is easily distinguishable from normal hemoglobin. The speed and simplicity of the method make it potentially attractive for large-scale population screening.

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“…6 Shortly thereafter, field desorption was displaced by more reliable techniques, including liquid secondary ion mass spectrometry (LSIMS), 5,7-9 fast atom bombardment (FAB), [10][11][12][13][14][15] and plasma desorption mass spectrometry (PDMS). 16…”

mentioning

confidence: 99%

Toward a Simple, Expedient, and Complete Analysis of Human Hemoglobin by MALDI-TOFMS

Houston

Reilly

1999

Anal. Chem.

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MALDI mass spectrometry is explored as a method for hemoglobin characterization. To simplify and expedite the analysis, hemoglobin is obtained without purification directly from whole human blood. The use of trypsinactivated bioreactive MALDI probes is evaluated as a means to further reduce the analysis time from hours to minutes. Moreover, variations of the MALDI matrix preparation facilitate detection of the problematic tryptic peptides alpha T12, alpha T13, and beta T12. The results reveal that MALDI-based methods are easily implemented, are rapid, and allow detection of traditionally elusive tryptic peptides.

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Plasma desorption mass spectrometry of haemoglobin tryptic peptides for the characterization of a Hungarian α-chain variant

Cited by 12 publications

References 27 publications

Studies of cisplatin and hemoglobin interactions using nanospray mass spectrometry and liquid chromatography with inductively-coupled plasma mass spectrometry

Studies of cisplatin and hemoglobin interactions using nanospray mass spectrometry and liquid chromatography with inductively-coupled plasma mass spectrometry

Rapid Analysis of Hemoglobin from Whole Human Blood by Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry

Toward a Simple, Expedient, and Complete Analysis of Human Hemoglobin by MALDI-TOFMS

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