Kinetics of the Carbamylation of the Amino Groups of Sickle Cell Hemoglobin by Cyanate

Lee, Choong K.; Manning, James M.

doi:10.1016/s0021-9258(19)43582-5

Cited by 58 publications

(13 citation statements)

References 16 publications

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“…d. Cyanates, Isocyanates, and Isothiocyanates  Urea and Thiourea Bond Formation. Carbamylation by potassium or sodium cyanate to yield 4.35 (eq 4.8) has been used for establishing structure/function relations in Hb, including determination of the residues involved in the Bohr effect, the role of the terminal NH 2 groups in CO 2 binding, the mechanism of the CO 2 -mediated reduction of O 2 affinity, and for increasing the O 2 affinity of HbS. ,,− …”

Section: Acylation Reactionsmentioning

confidence: 99%

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: Acylation Reactionsmentioning

confidence: 99%

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

2001

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“…In the first step, −COOH groups in PAA were activated using 1-ethyl-3(3-(dimethylamino)propyl) carbodiimide (EDC) and coupled with amino groups of lysine side chains on Hb to produce Hb–PAA. Typically mammalian Hb has nearly 44 lysine residues. , In the second step, the Hb–PAA conjugates were reacted with EtOH or 1-prop to form the corresponding Hb–PAA–Eth and Hb–PAA–1-prop, respectively.…”

Section: Introductionmentioning

confidence: 99%

“…Typically mammalian Hb has nearly 44 lysine residues. 30,31 In the second step, the Hb−PAA conjugates were reacted with EtOH or 1-prop to form the corresponding Hb−PAA−Eth and Hb−PAA−1-prop, respectively.…”

Section: Introductionmentioning

confidence: 99%

Efficient Biocatalysis in Organic Media with Hemoglobin and Poly(acrylic acid) Nanogels

et al. 2014

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We previously reported that the stability and aqueous catalytic activity of met-hemoglobin (Hb) was improved when covalently conjugated with poly(acrylic acid) (PAA). In the current study, the Hb-PAA-water interface was modified to improve Hb catalytic efficiency in organic solvents (0-80% v/v organic solvent; remainder is the conjugate, the substrate, and water). The protein-polymer-solvent interface modification was achieved by esterifying the carboxylic acid groups of Hb-PAA with ethanol (EtOH) or 1-propanol (1-prop) after activation with carbodiimide. The resulting esters (Hb-PAA-Eth and Hb-PAA-1-prop, respectively) showed high peroxidase-like catalytic activities in acetonitrile (ACN), dimethylformamide (DMF), EtOH, and methanol (MeOH). Catalytic activities depended on the log(P) values of the solvents, which is a measure of solvent lipophilicity. The highest weighted-average activities were noted in MeOH for all three conjugates, and the lowest average activities were noted in DMF for two of the conjugates. Interestingly, the average activities of the conjugates were higher than that of Hb in all solvents except in ACN. The ratio of the catalytic rate constant (kcat) to the Michaelis constant (KM), the catalytic efficiency, for Hb-PAA-Eth in MeOH was the highest noted, and it is ~3-fold higher than that of Hb in buffer; conjugates offered higher efficiencies than Hb at most solvent compositions. This is the very first general, versatile, modular strategy of coupling the enhanced stability of Hb with improved activity in organic solvents via the chemical manipulation of the polymer shell around Hb and provides a robust approach to efficient biocatalysis in organic solvents.

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“…the oxygen affinity of HbS (Kilmartin and Rossi-Bernardi, 1969;Diederich, 1972;May et al, 1972) as well as the survival of HbS-containing red cells (Gillette et al, 1971). There have been several studies (Lee and Manning, 1973;Njikam et al, 1973;Nigen et al, 1974;Williams et al, 1975) of the chemistry of the cyanate carbamoylation of hemoglobins, reportedly identical in HbS and in HbA,2 as well as of the kinetics of the carbamoylation reaction itself. The reaction occurs more extensively at the NH2 terminals of deoxy than of oxyhemoglobin, also favoring « over ß chain NH2 terminals in the deoxy but not the oxy case.…”

mentioning

confidence: 99%

“…For analysis purposes, the carbamoylated hemoglobin was isolated according to Williams et al (1975). Only N-terminally modified hemoglobin was detectable; upon analysis, this contained one carbamoyl group per heme, as measured by valine hydantoin (Lee and Manning, 1973).4 No hemoglobin partially or totally carbamoylated on the lysine C-NH2 groups was present, as indicated by the absence of more slowly elutable absorption peaks. Thus, as observed earlier by others, under these experimental conditions (Njikam et al, 1973;Nigen et al, 1974;Williams et al, 1975), only N-terminal carbamoylation is detectable.…”

mentioning

confidence: 99%

Circular dichroism studies of cyanate-induced conformational changes in hemoglobins A and S

Simons¹,

Hartzband²,

Whitin³

et al. 1976

Biochemistry

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Kinetics of the Carbamylation of the Amino Groups of Sickle Cell Hemoglobin by Cyanate

Cited by 58 publications

References 16 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

Efficient Biocatalysis in Organic Media with Hemoglobin and Poly(acrylic acid) Nanogels

Circular dichroism studies of cyanate-induced conformational changes in hemoglobins A and S

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