• Cytoplasmic Fragment
    • Robert Cassoly
    • Robert Cassoly: Influence Statistics

      Robert Cassoly

      Robert Cassoly

      Laboratoire de Biologie Cellulaire des Membranes, Institut Jacques Monod, UMR 7592, CNRS, Universités Paris VI et Paris VII, F-75005 Paris, France | From the Laboratoire ...

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      Robert Cassoly:Expert Impact

      Concepts for whichRobert Cassolyhas direct influence:Cytoplasmic fragment,3 protein,Band 3 protein,Erythrocyte membrane,Sickle cells,Human hemoglobin,Hemoglobins humans,Valency hybrids.

      Robert Cassoly:KOL impact

      Concepts related to the work of other authors for whichfor which Robert Cassoly has influence:Nitric oxide,Band 3,Erythrocyte membrane,Human hemoglobin,Blood cells,Cytoplasmic domain,Protein binding.

      KOL Resume for Robert Cassoly


      Laboratoire de Biologie Cellulaire des Membranes, Institut Jacques Monod, UMR 7592, CNRS, Universités Paris VI et Paris VII, F-75005 Paris, France


      From the Laboratoire Physiopathologie Cardiovasculaire (I.K., M.P., G.V.), INSERM U-390, Hôpital Arnaud de Villeneuve, Montpellier, France, and Institut Jacques Monod (R.C.), CNRS UMR 9922, Universite Paris-7.

      Institut Jacques Monod, CNRS Unité Mixte de Recherche 9922, Université Paris-7, 75251 Paris, France


      Institut Jacques Monod, CNRS‐Université Paris VII. Paris, France


      Hop Bicetre, INSERM, U299, F 94275 LE Kremlin Bicetr, France; Hop Port Royal, INSERM, U29, F 75014 Paris, France and Inst J Monod, CNRS, UMR 9922, F 75005 Paris, France


      Laboratorie de Biophysique, Institut de Biologie Physico‐Chimique, 13, rue Pierre et Marie Curie, 75005 Paris, France


      Veterans Administration Medical Center, Omaha, Nebraska.

      Institut de Biologie Physico-Chimique, Laboratoire de Biophysique, 13, rue Pierre et Marie Curie, 75005 Paris, France


      Laboratoire de Biophysique, Unité associée 1089 du Centre National de la Recherche Scientifique, Institut de Bioiogie Physico‐Chimique, Paris


      Institut de Biologie Physico-chimique, 75005 Paris France


      Laboratoire de Biophysique, Institut de Biologie Physico-Chimique, rue Pierre et Marie Curie, 75005 Paris France


      Institut de Biologie Physico-chimique, 13, rue Pierre et Marie Curie, 75005 Paris, France


      Université Claude Bernard, Institut de Biologie Physico-chimique, Laboratoire de Biophysique, 13, rue Pierre et Marie Curie, 75005 Paris, France


      Institut de Biologie Physico-chimique, 13, rue Pierre et Marie Curie, F-75005 Paris, France


      Institut de Biologie Physico-chimique, 13, Rue Pierre et Marie Curie, F-75005 Paris, France


      Institut de Biologie Physico‐Chimique, 13 Rue Pierre‐et‐Maric‐Curie, F‐75231 Paris‐Cedex‐05. France


      Institut de Biologie Physico-chimique, 13 rue Pierre et Marie Curie 75005 Paris, France


      Institut de Biologie Physico‐Chimique 13 Rue Pierre‐et‐Marie‐Curie, F‐75005 Paris, France


      From the Section of Biochemistry and Molecular Biology, Cornell University, Ithaca, New York 14850


      Department of Biochemistry and Molecular Biology Wing Hall, Cornell University Ithaca, New York 14850, USA


      Institut de Biologie Physico-Chimique 13, rue Pierre et Marie Curie, Paris 5 °, France


      Institut de Biologie Physico-Chimique, Paris (France)


      Institut de Biologie Physicochimique, 13, rue Pierre et Marie Curie Paris 5 France

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      Sample of concepts for which Robert Cassoly is among the top experts in the world.
      Concept World rank
      chain semihbβ #1
      celui méthémoglobine #1
      effects nonsaturating amounts #1
      heterotetramers relaxation time #1
      properties valency #1
      difficulty artificial analogs #1
      hbno perutz #1
      hbno β2deoxy hybrid #1
      outward water permeability #1
      hbno α2no #1
      spin ankyrin #1
      hbno induced #1
      densityseparated cell fractions #1
      gap restoration #1
      50ml erythrocyte suspension #1
      hemoprotein gel filtration #1
      toxic photoactivated radicals #1
      small amounts hemoprotein #1
      fragment flash photolysis #1
      methemoglobin apomyoglobin #1
      direct determination l′4 #1
      monoxide semihemoglobins #1
      cnbractivated sepharose matrix #1
      methemoglobin hemoprotein #1
      dimer hemoglobin #1
      enucleated mixing #1
      criteria quaternary structure #1
      betah2o #1
      oxygenation behavior #1
      10 mmphosphate buffer #1
      actin tubulin form #1
      composé hémoglobinique #1
      semihbβ α #1
      hemoglobin nitrosyl hbno #1
      spontaneous microvesiculization #1
      study hemoglobin properties #1
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      Prominent publications by Robert Cassoly

      KOL-Index: 8614

      The cytoplasmic fragment of band 3 protein isolated from the human erythrocyte membrane was linked to a CNBr-activated Sepharose matrix in an attempt to measure, in batch experiments, its equilibrium binding constant with oxy- and deoxyhemoglobin at physiological pH and ionic strength values and in the presence or the absence of 2,3-diphosphoglycerate. All the experiments were done at pH 7.2, and equilibrium constants were computed on the basis of one hemoglobin tetramer bound per ...

      Known for Band 3 | Ionic Strength | Human Erythrocyte | Cytoplasmic Fragment | Bound Proteins
      KOL-Index: 8545

      The time course of carbon monoxide binding to stripped valency hybrids (α ii β iii CN)2 and (α iii CNβ ii )2 was studied at pH 6.6 and T = 0.05. It exhibits a strong heterogeneous character. Two spectrophotometrically and kinetically distinct forms are apparent. At most wave lengths the fast component contributes about 60 to 80% of the total absorbance change and has a rate of binding similar to that of rapid hemoglobins. Correlation between the spectral properties of hybrids and their ...

      Known for Valency Hybrids | Ligand Binding | Carbon Monoxide | Organic Phosphates | Rapid Equilibrium
      KOL-Index: 8184

      Binding of the cytoplasmic fragment of band 3 protein to oxyhemoglobin in solution caused a spectral change in the absorbance of the hemoglobin beta chain at a ratio of one monomer of band 3 protein per alpha beta dimer of hemoglobin. This spectral change was reversed at higher ratios of cytoplasmic fragment to hemoglobin. The unusual dependence on protein concentration was interpreted as indicating the formation of higher aggregates of the complex between hemoglobin and the cytoplasmic ...

      Known for 3 Protein | Cytoplasmic Fragment | 1 Erythrocyte | Anion Exchange | Hemoglobins Humans
      KOL-Index: 8108

      The association of the isolated cytoplasmic fragment of band 3 protein with human hemoglobin was studied by rate zonal centrifugation in sucrose density gradients, by quenching of fragment fluorescence by hemoglobin, and by flash photolysis of carbon monoxidebound hemoglobin as a function of fragment concentration. The centrifugation results showed that both proteins interact and that the interaction is abolished upon addition of glyceraldehyde-3-phosphate dehydrogenase. The fractions ...

      Known for Cytoplasmic Fragment | 3 Protein | Human Hemoglobin | Alpha Beta Dimer | Density Gradient
      KOL-Index: 7894

      The identification of the protein that exerts the function of Cl-/HCO3- exchange is still unresolved in cardiac tissue. We have addressed this issue by using a multiple technical approach. Western blotting analysis with an antibody raised against human erythroid whole band 3 protein, the so-called protein that mediates the Cl-/HCO3- exchange in erythrocytes, showed that adult cardiomyocytes expressed two proteins immunologically related to the erythroid band 3. These proteins migrated in ...

      Known for Band 3 | Exchange Protein | Adult Cardiomyocytes | Confocal Microscopy | 80 120
      KOL-Index: 7605

      Spectrin extracted from human red blood cells has been spin labeled in its dimeric and tetrameric forms with five different nitroxide derivatives of increasing chain length between their maleimide binding group and their nitroxide reporter group. Three molecules of spin label are bound per spectrin dimer. Electron spin resonance spectra show the simultaneous presence of strongly and weakly immobilized spin labels. Their relative proportion depends on the label length and is suddenly ...

      Known for Erythrocyte Membrane | Spin Label | Higher Temperatures | Conformation Spectrin | Resonance Spectroscopy
      KOL-Index: 7106

      Hemoglobin binds to the cytoplasmic domain of band 3 protein (CDB3) at physiologic pH and ionic strength in an oxygen-linked fashion, with deoxyhemoglobin having the higher affinity. The evidence in the literature suggests functional communication between the hemoglobin-binding site on CDB3 and the anion transport sites within the membrane-bound domain of band 3. Since the hemoglobin-binding site is estimated to be over 200 A from the transport domain, the functional communication ...

      Known for Hemoglobin Binding | 3 Protein | Sulfhydryl Groups | Cytoplasmic Domain Band | Anion Transport
      KOL-Index: 6950

      The addition of inositolhexaphosphate to stripped nitrosyl hemoglobin provokes strong changes in the visible absorption spectrum of the protein. The stoichiometry of this reaction, determined by spectrophotometry, is one mole of IHP per tetramer. The equilibrium dissociation constant of IHP for HbNO, in 0·1 m-2,2-bis (hydroxymethyl)-2,2′,2″-nitrilotriethanol (pH 6·8) is 1·3×10−6 m and increases with ionic strength and pH. IHP has only a small effect on bis (N-maleimidomethyl) ether ...

      Known for Optical Spectrum | Nitrosyl Hemoglobin | Protein Binding | Spectrophotometry Ultraviolet | Quaternary Structure
      KOL-Index: 6836

      Human hemoglobin has been labeled on cysteine 93(beta) with the maleimide spin label, 3-maleimido-2,2,5,5-tetramethyl-1-pyrrolidinyloxyl and reassociated with erythrocyte membrane previously stripped of hemoglobin and glyceraldehyde-3-phosphate dehydrogenase. The affinity of hemoglobin for the membrane is not affected by the presence of the label. Saturation transfer electron paramagnetic resonance measurements show that the diffusion rotational movements of hemoglobin are considerably ...

      Known for Erythrocyte Membrane | Electron Paramagnetic | Human Hemoglobin | Spin Resonance | 3 Protein
      KOL-Index: 6802

      The preparation and some properties of valency hybrids derived from human hemoglobin are described. These derivatives (α23+ β22+ and α22+ β23+), containing both the chains of a given type (α or β) in the ferri state, are obtained through association of isolated partner chains, each in the desired valency state. The hybrids are stable and are tetramers in the normal pH range. The oxygenation behavior of the hybrids has been studied at different pH values; the two complementary valency ...

      Known for Human Hemoglobin | Valency Hybrids | Β Chains | Oxygen Equilibria | Preparation Properties
      KOL-Index: 6618

      There does not appear to be any co-operativity manifest in the four combination rate constants for the binding of nitric oxide to deoxyhemoglobin. The time-course of the observed reaction is best fitted by statistically related rates, and the numerical relation between the rate constants for the binding of the fourth molecule of carbon monoxide and the fourth molecule of nitric oxide, which can be obtained independently, also argues for a statistical relation between the nitric oxide ...

      Known for Carbon Monoxide | Human Hemoglobin | Nitric Oxide | Kinetics Ligands | Rate Constants
      KOL-Index: 6158

      The binding of various linear and branched chain alkylisocyanides to soybean leghemoglobin has been studied with respect to association and dissociation kinetics and the results compared with those obtained in parallel on sperm whale and horse heart myoglobins; the linear ligands used (methyl to n-heptyl) cover a greater distribution of chain lengths than hitherto used. The association rate constants are much higher for leghemoglobin than for myoglobin, while the dissociation rates are ...

      Known for Soybean Leghemoglobin | Whale Myoglobin | Rate Constants | Protein Binding | Alkyl Chain
      KOL-Index: 5939

      Semihemoglobins α and β are derivatives of human hemoglobin which possess the usual chain composition (α2β2 or αβ) but which carry the heme prosthetic group on only one kind of chain (α or β), the complementary chain (β° or α°) being heme-free. In this paper, new results on two compounds of this type, namely, semiHbαD (αβ°) and semiHbβ (α°β) have been presented; existing data on other earlier preparations have also been reviewed. Methods for preparation of semiHbαD and semiHbβ have been ...

      Known for Α Β | Heme Prosthetic | Human Hemoglobin | Carbon Monoxide | Oxygen Equilibrium
      KOL-Index: 5592

      The effects of organic phosphates on the carbon monoxide binding and NMR spectra of the hemoglobin valency hybrids (αIIICN βII)2 and (αIIβIIICN)2, have been studied. The stripped deoxy hybrids show heterogeneity in kinetics with two spectrophotometrically distinct forms which are not in rapid equilibrium. At most wavelengths the fast component contributes about 60 to 80% of the total absorbance change and has a rate of binding similar to that of isolated chains or other rapid ...

      Known for Binding Kinetics | Nmr Spectra | Organic Phosphates | Valency Hybrids | Fast Component
      KOL-Index: 5265

      Isolated human erythrocyte spectrin, ankyrin, and protein 4.1 have been labeled with the maleimide spin label, 3-maleimido-2,2,5,5-tetramethyl-1-pyrrolidinyloxyl, and studied by saturation transfer electron paramagnetic resonance spectroscopy. The presence of the labels does not affect the reassociation of these proteins with erythrocyte membranes selectively depleted of either spectrin-actin or of all the extrinsic proteins. When maleimide spin-labeled spectrin is reassociated with the ...

      Known for Human Erythrocyte | Membrane Proteins | Labeled Spectrin | Protein 41 | Electron Spin

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      Laboratoire de Biologie Cellulaire des Membranes, Institut Jacques Monod, UMR 7592, CNRS, Universités Paris VI et Paris VII, F-75005 Paris, France | From the Laboratoire Physiopathologie Cardiovasculaire (I.K., M.P., G.V.), INSERM U-390, Hôpital Arn

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