Cross-linking of stroma-free hemoglobin monitored by high-performance liquid chromatography

Pietta, Piergiorgio; Calatroni, Alma; Palazzini, Gabriele; Agostoni, A

doi:10.1016/s0021-9673(00)82782-x

Cited by 3 publications

(3 citation statements)

References 12 publications

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“…Chromatography, electrophoresis, gel isoelectric focusing, and other techniques have confirmed the polydispersity, heterogeneity, and dependence on experimental conditions of glutaraldehyde-polymerized Hb. ,,,,,,,, The reaction products comprised unreacted Hb and species that were intra- and intermolecularly cross-linked at various sites and to various degrees. MetHb formation was usually important but could be limited by addition of l -ascorbic acid to the reaction mixture. , Viscosity increased rapidly with Hb concentration, further reflecting lack of molecular uniformity. , There still exists considerable uncertainty about the reaction sites, number and identity of the groups involved in cross-linking, mechanisms of reaction, chemical constitution, and evolution of such products.…”

Section: Polymerizationmentioning

confidence: 87%

“…522 Chromatography, electrophoresis, gel isoelectric focusing, and other techniques have confirmed the polydispersity, heterogeneity, and dependence on experimental conditions of glutaraldehyde-polymerized Hb. 524,729,769,771,772,775,776,790,791 The reaction products comprised unreacted Hb and species that were intra-and intermolecularly cross-linked at various sites and to various degrees. MetHb formation was usually important but could be limited by addition of L-ascorbic acid to the reaction mixture.…”

Section: Polymerizationmentioning

confidence: 99%

“…MetHb formation was usually important but could be limited by addition of L-ascorbic acid to the reaction mixture. 521,791 Viscosity increased rapidly with Hb concentration, further reflecting lack of molecular uniformity. 569,774 There still exists considerable uncertainty about the reaction sites, number and identity of the groups involved in cross-linking, mechanisms of reaction, chemical constitution, and evolution of such products.…”

Section: Polymerizationmentioning

confidence: 99%

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Oxygen Carriers (“Blood Substitutes”)Raison d'Etre, Chemistry, and Some PhysiologyBlut ist ein ganz besondrer Saft

2001

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Pharmaceutical Corporation in San Diego; however, the opinion expressed here are solely his and not necessarily those of the Corporation. Jean G. Riess received his chemical engineer and doctorat-e `s-sciences degrees (the latter with Professor Guy Ourisson in 1963) from the University of Strasbourg. He then spent two years with John Van Wazer at Monsanto in Saint-Louis, MO, learning some phosphorus and transitionmetal chemistry. In 1968 he became Professor at the University of Nice, France, where he founded, directed, and eventually became honorary director of the Unite ´de Chimie Mole ´culaire (associated with the Centre National de la Recherche Scientifique). His research successively involved phosphorus chemistry, transition-metal chemistry, organometallics, and eventually perfluorochemicals. His present interests are in fluorocarbons, fluorinated amphiphiles, and their colloid chemistry, including fluorocarbon emulsions for in vivo O 2 delivery, fluorinated self-assemblies, and drug delivery systems. Professor Riess has published about 360 papers and holds ca. 25 patents. He has served on numerous councils and committees and has chaired or co-chaired international conferences on phosphorus chemistry and blood substitutes. He has won awards from the French Academy of Sciences, French Chemical Society, Alexander von Humboldt Stifftung, City of Nice and Controlled Release Society, as well as Alliance's first Distinguished Contribution Award. He holds an honorary Research Associate position at the University of California at San Diego and sits on the Board of Directors of Alliance Pharmaceutical Corp.

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Section: Polymerizationmentioning

confidence: 87%

Section: Polymerizationmentioning

confidence: 99%

Section: Polymerizationmentioning

confidence: 99%

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Oxygen Carriers (“Blood Substitutes”)Raison d'Etre, Chemistry, and Some PhysiologyBlut ist ein ganz besondrer Saft

2001

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Characterization of the Chemical Architecture of Carbon-Fiber Microelectrodes. 3. Effect of Charge on the Electron-Transfer Properties of ECL Reactions

Hopper¹,

Kuhr²

1994

Anal. Chem.

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Two techniques, cyclic voltammetry and the microscopic imaging of electrochemically generated chemiluminescence (ECL), have been used to evaluate the effectiveness of various electrochemical pretreatments on the electron-transfer properties of carbon-fiber microelectrodes. The surfaces of carbon-fiber microelectrodes were electrochemically treated to produce different levels of surface oxides in the following manner: after normal polishing and cleaning in hot toluene and water, the carbon surface was activated by applying a cyclic potential from -0.2 to 2.0 V at a frequency of 50 Hz for 3 s in solutions of varying pH: 1M HCl, pH 7.4 and pH 12.0 phosphate buffers. Cyclic voltammetry was employed to elucidate the effect of the surface pretreatment on the overall voltammetric properties of the different pretreatment methods. The ECL emission intensity was imaged with resolution on the submicrometer scale with a conventional fluorescence microscope equipped with a cooled, slow-scan CCD camera. In addition to investigating pretreatment effects with luminol, we have also examined the ECL properties of a positively charged species, ruthenium tris (2,2'-bipyridine) dichloride hexahydrate, whose luminescent properties are also well documented. Such information is not only invaluable for the rational design of surface-modified ultramicroelectrodes, but it can also yield considerable information concerning the surface interactions influencing organic electron-transfer reactions at carbon surfaces.

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Comparison of the Properties of Human Hemoglobin Covalently Bound to Carboxyl Dextrans with Free and Polymerized Hemoglobin

Pace

Palazzini

et al. 1984

Preparative Biochemistry

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Human stroma-free hemoglobin (SFH) was coupled in the oxy or deoxy conformations to carboxyldextrans through amide bonds. The complexes were analysed by gel permeation high performance chromatography, and their molecular mass distribution ranged from 90,000 to 300,000. Covalent coupling of SFH to carboxyldextrans determined an increase of the oxygen affinity when compared to free SFH. The P50 of the complex formed from carboxyldextrans and SFH in the oxy state was lower than that of the derivative obtained from SFH in the reduced state. On the other hand, glutaraldehyde cross-linked SFH still showed cooperativity when reacted in the deoxy state and in the presence of pyridoxal phosphate, and its oxygen affinity was similar to that of the free pyridoxylated SFH. These results lead to exclude the potential use of these dextran-SFH complexes as oxygen carriers.

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Cross-linking of stroma-free hemoglobin monitored by high-performance liquid chromatography

Cited by 3 publications

References 12 publications

Oxygen Carriers (“Blood Substitutes”)Raison d'Etre, Chemistry, and Some PhysiologyBlut ist ein ganz besondrer Saft

Oxygen Carriers (“Blood Substitutes”)Raison d'Etre, Chemistry, and Some PhysiologyBlut ist ein ganz besondrer Saft

Characterization of the Chemical Architecture of Carbon-Fiber Microelectrodes. 3. Effect of Charge on the Electron-Transfer Properties of ECL Reactions

Comparison of the Properties of Human Hemoglobin Covalently Bound to Carboxyl Dextrans with Free and Polymerized Hemoglobin

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