Detection of a Novel Variant Human Hemoglobin by Electrospray Ionization Mass Spectrometry

Troxler, Heinz; Neuheiser, F.; Kleinert, P.; Kuster, Thomas; Heizmann, Claus W.; Sack, Ragna; Hunziker, Peter; Neuhaus, Thomas J.; Schmid, Marlis; Frischknecht, Hannes

doi:10.1006/bbrc.2002.6762

Cited by 14 publications

(7 citation statements)

References 10 publications

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“…During this study, 2 new chromatographically silent Hb variants, Hb Zurich-Hottingen (24 ) and Hb Zurich-Langstrasse, were detected. Both showed no abnormalities as analyzed by cation-exchange HPLC, RP HPLC, or IEF.…”

Section: Zurich-langstrassementioning

confidence: 85%

Mass Spectrometry: A Tool for Enhanced Detection of Hemoglobin Variants

Kleinert¹,

Schmid

Zurbriggen

et al. 2008

Clinical Chemistry

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Section: Zurich-langstrassementioning

confidence: 85%

Mass Spectrometry: A Tool for Enhanced Detection of Hemoglobin Variants

Kleinert¹,

Schmid

Zurbriggen

et al. 2008

Clinical Chemistry

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“…As commonly found in the case of other hemoglobins, neither NHb tetramers nor the holoprotein forms of α-chains or β-chains could be distinguished from noise. The heme-free α-chains of NHb were unmodified [ m / z 15125 ± 1 (found), m / z 15126 (reported) , ], while the heme-free β-chains appeared to contain at least one modification [ m / z 15934 ± 1 (found), m / z 15867 (reported) , ]. The additional 67 amu per β-chain corresponds to substitution of one H with NO 2 (+46 − 1) and replacement of H + with Na + (+22 − 1) during ionization.…”

Section: Resultsmentioning

confidence: 99%

Covalent Modifications of Hemoglobin by Nitrite Anion: Formation Kinetics and Properties of Nitrihemoglobin

Otsuka

Marks

Winnica

et al. 2010

Chem. Res. Toxicol.

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The green nitrihemoglobin (α2β2 tetramer, NHb) was prepared by the aerobic reaction of excess nitrite with human hemoglobin A0 under mildly acidic conditions. A rate equation was determined and found to depend on nitrite, hydrogen ion and oxygen concentrations: –d[HbNO2]/dt = (k1 + k2(Ka[HNO2])[O2]1/2)•[ HbNO2], where k1 = 2.4 (±0.9) × 10-4 s-1, k2 = 1 (±0.2) × 105 M-5/2s-1 and Ka is the acid dissociation constant for nitrous acid (4.5 × 10-4 M). Also, the chemical properties of NHb are compared to those of the normal hemoglobin (including the addition products of both common oxidation states with exogenous ligands, the alkaline transitions of the ferric forms and the oxygen binding characteristics of the ferrous forms) and were found to be nearly indistinguishable. Therefore, the replacement of a single vinyl hydrogen with a nitro group on the periphery of each macrocycle in hemoglobin does not significantly perturb the interaction between the hemes and the heme pockets. Since non-photochemical reaction chemistry must necessarily be most dependent on electronic ground states, it follows that the clearly visible difference in color between hemoglobin A0 and NHb must be associated primarily with the respective electronic excited states. The possibility of NHb formation in vivo and its likely consequences are considered.

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“…Specifically, the quaternary structure of Hb comprises two pairs of heme‐containing α‐ and β‐ or δ‐subunits in a tetrahedral arrangement. The non‐covalent bonds stabilizing the complex ( via non‐polar and van der Waals interactions, hydrogen bonds, and salt bridges) can be easily overcome, leading to the reversible dissociation of Hb and its synthetic analogs into dimers and monomers 12, 20–22. Under acidic and alcoholic conditions, such as those in the sheath liquid, monomers of Hb were detected due to in‐Taylor cone dissociation of the tetramers.…”

Section: Resultsmentioning

confidence: 99%

Analysis of hemoglobin‐based oxygen carriers by CE‐UV/Vis and CE‐ESI‐TOF/MS

et al. 2010

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Blood doping involves the use of products that enhance the uptake, transport, or delivery of oxygen to the blood. One approach uses artificial oxygen carriers, known as hemoglobin-based oxygen carriers (HBOCs). This study describes an analytical strategy based on CE for detecting intact HBOCs in plasma samples collected for doping control. On-capillary detection was performed by UV/Vis at 415 nm, which offered detection selectivity for hemoproteins (such as hemoglobin and HBOCs). On-line ESI-MS detection with a TOF analyzer was further used to provide accurate masses on CE peaks and to confirm the presence of HBOCs. An immunodepletion sample preparation step was mandatory prior to analysis, in order to remove most abundant proteins that interfered with CE separation and altered the ESI process. This analytical method was successfully applied to plasma samples enriched with Oxyglobin, a commercially available HBOC used for veterinary purposes. Detection limits of 0.20 and 0.45 g/dL were achieved in plasma for CE-UV/Vis at 415 nm and CE-ESI-TOF/MS, respectively.

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Detection of a Novel Variant Human Hemoglobin by Electrospray Ionization Mass Spectrometry

Cited by 14 publications

References 10 publications

Mass Spectrometry: A Tool for Enhanced Detection of Hemoglobin Variants

Mass Spectrometry: A Tool for Enhanced Detection of Hemoglobin Variants

Covalent Modifications of Hemoglobin by Nitrite Anion: Formation Kinetics and Properties of Nitrihemoglobin

Analysis of hemoglobin‐based oxygen carriers by CE‐UV/Vis and CE‐ESI‐TOF/MS

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