Substituts des globules rouges: émulsions de fluorocarbures et solutions d'hémoglobine

Remy, Bernadette; Deby‐Dupont, G.; D'Ans, V.; Ernest, Philippe; Lamy, Maurice

doi:10.1016/s0750-7658(99)90155-7

Annales Françaises d'Anesthésie et de Réanimation

1999

DOI: 10.1016/s0750-7658(99)90155-7

|View full text |Cite

Substituts des globules rouges: émulsions de fluorocarbures et solutions d'hémoglobine

Bernadette Remy

G. Deby‐Dupont

V. D'Ans

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2004

2014

Publication Types

Select...

Article3

Relationship

Self Cite0

Independent3

Authors

Journals

Cited by 3 publications

(1 citation statement)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The development of new drugs to rectify the lack of available whole blood was required. Blood substitutes can be either synthetic perfluorocarbon solutions or hemoglobin-based oxygen carriers (HBOCs) . First studies on “artificial blood” have led to administration of purified hemoglobin solutions. , Although showing promising results, cell-free hemoglobin tetrameric structure can dissociate in plasma into α,β-dimers, causing nephrotoxicity .…”

mentioning

confidence: 99%

Simple Identification of A Cross-Linked Hemoglobin by Tandem Mass Spectrometry in Human Serum

et al. 2004

View full text Add to dashboard Cite

Hemoglobin-based oxygen therapeutics are prepared by reaction of hemoglobin with cross-linking molecules and are utilized as blood substitutes. They can be used as doping agents to increase the oxygen-carrying capacity of hemoglobin. We have compared a glutaraldehyde-polymerized bovine hemoglobin (Oxyglobin, Biopure Corp.) with natural bovine hemoglobin by mass spectrometry in order to detect specific fragment ions of the cross-linked protein for further potential applications in doping control of human blood samples. HCl acid (6 N) hydrolysis was performed in parallel on both proteins. Hydrolysates were then analyzed by direct infusion electrospray mass spectrometry (ESIMS) using a triple quadrupole mass spectrometer. Confirmation and precision were obtained by LC-ESIMS(n) experiments performed on an ion trap mass spectrometer. Chromatographic and mass spectrometry data allowed detection of two potential Oxyglobin-specific ions--m/z 299 and 399--that were shown to lose a 159 u neutral fragment under collision-induced dissociation conditions. Thus, monitoring of constant neutral loss of 159 u on acid hydrolysates of human serum samples spiked with different amounts of Oxyglobin has proved to be an efficient screening method to specifically detect and identify Oxyglobin. LC-MS of the spiked serum sample hydrolysates enabled detection of Oxyglobin at a detection limit of 4 g x L(-1).

show abstract

mentioning

confidence: 99%

Simple Identification of A Cross-Linked Hemoglobin by Tandem Mass Spectrometry in Human Serum

et al. 2004

View full text Add to dashboard Cite

show abstract

N-Terminal Adducts of Bovine Hemoglobin with Glutaraldehyde in a Hemoglobin-Based Oxygen Carrier

2005

View full text Add to dashboard Cite

Hemoglobin-based oxygen carriers (HBOCs) are being developed for the medical field, but because they could increase an athlete's performance, they are misapplied for doping purposes. We previously presented a screening method to detect Oxyglobin (Biopure Corp.) and PolyHeme (Northfield Laboratories Inc.) in serum samples using total acid hydrolysis followed by electrospray mass spectrometry analyses. An alternative mass spectrometric method involving enzymatic hydrolysis is here presented. Digestion of Oxyglobin by endoproteinase Glu-C and LC/MS analyses of the mixture allowed the detection of unique peptidic fragments in comparison with a bovine hemoglobin digest. Tandem mass spectrometry experiments of these peptide ions were performed, and two specific species were actually identified as the N-terminal enzymatic fragment of the beta chain carrying two different modifications. Sequential MS3 experiments using an ion trap mass spectrometer permitted us to locate the chemical modification by the glutaraldehyde on the NH2-terminal group and to propose a structure for the modified peptides. In another set of experiments, screening of these two diagnostic ions into Oxyglobin-spiked serums using precursor ion scan mode in a triple quadrupole instrument allowed the detection of this HBOC with a detection limit of 2 g L(-1).

show abstract

Liquid Perfluorochemicals as Flexible and Efficient Gas Carriers Applied in Bioprocess Engineering: An Updated Overview and Future Prospects

Pilarek¹

2014

Chemical and Process Engineering

View full text Add to dashboard Cite

Fully synthetic, biochemically inert and water-immiscible liquid perfluorochemicals (PFCs) are recognised as flexible liquid carriers/scavengers of gaseous compounds (respiratory gases mainly, i.e. O 2 and CO 2 ) and increasingly applied in bioprocess engineering. A range of unmatched physicochemical properties of liquid PFCs, i.e. outstanding chemo-and thermostability, extremely low surface tension, simultaneous hydro-and lipophobicity, which result from carbon chain substitution with fluorine atoms (the most electronegative chemical element) and the presence of intramolecular C-F bonds (the strongest single bond known in organic chemistry) have been described in detail. Exceptional propensity to solubility of respiratory gases in liquid perfluorinated compounds has been widely discussed. Advantages and disadvantages of bioprocess applications of liquid PFCs in the form of a pure PFC as well as in an emulsified form have been pointed out. A liquid PFC-mediated mass transfer intensification in various types of microbial, plant cell and animal cell culture systems: from miniaturised microlitre-scale cultures, via biomaterial-based scaffolds containing culture systems, to litre-scale bioreactors, has been reviewed and elaborated on bearing in mind the benefits of bioprocesses.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Substituts des globules rouges: émulsions de fluorocarbures et solutions d'hémoglobine

Cited by 3 publications

References 49 publications

Simple Identification of A Cross-Linked Hemoglobin by Tandem Mass Spectrometry in Human Serum

Simple Identification of A Cross-Linked Hemoglobin by Tandem Mass Spectrometry in Human Serum

N-Terminal Adducts of Bovine Hemoglobin with Glutaraldehyde in a Hemoglobin-Based Oxygen Carrier

Liquid Perfluorochemicals as Flexible and Efficient Gas Carriers Applied in Bioprocess Engineering: An Updated Overview and Future Prospects

Contact Info

Product

Resources

About