1981
[29] Measurement of CO2 binding: The 13C NMR method
Morrow J, Matthew J, Gurd F. [29] Measurement of CO2 binding: The 13C NMR method. Methods In Enzymology 1981, 76: 496-511. PMID: 6799730, DOI: 10.1016/0076-6879(81)76139-1.Peer-Reviewed Original ResearchMeSH KeywordsBicarbonatesCarbon DioxideHemoglobinsHumansHydrogen-Ion ConcentrationKineticsMagnetic Resonance SpectroscopyConceptsCarbamino adductsSingle carbon resonancesSensitivity of NMRNuclear magnetic resonance methodsUnique chemical speciesNMR spectraNMR methodsMagnetic resonance methodsR-NHNMR experimentsChemical speciesForm of CO2NMR spectrometerProtein samplesAdductsNMRFree induction decay signalResonance methodProteinCO2Average lifetimePowerful methodDecay signalResonanceMeasurements of CO2
1977
Quantitative determination of carbamino adducts of alpha and beta chains in human adult hemoglobin in presence and absence of carbon monoxide and 2,3-diphosphoglycerate.
Matthew J, Morrow J, Wittebort R, Gurd F. Quantitative determination of carbamino adducts of alpha and beta chains in human adult hemoglobin in presence and absence of carbon monoxide and 2,3-diphosphoglycerate. Journal Of Biological Chemistry 1977, 252: 2234-2244. PMID: 14958, DOI: 10.1016/s0021-9258(17)40546-1.Peer-Reviewed Original Research
1976
Carbon 13 resonances of 13CO2 carbamino adducts of alpha and beta chains in human adult hemoglobin.
Morrow J, Matthew J, Wittebort R, Gurd F. Carbon 13 resonances of 13CO2 carbamino adducts of alpha and beta chains in human adult hemoglobin. Journal Of Biological Chemistry 1976, 251: 477-484. PMID: 1395, DOI: 10.1016/s0021-9258(17)33904-2.Peer-Reviewed Original Research
1974
CO2 Adducts of Certain Amino Acids, Peptides, and Sperm Whale Myoglobin Studied by Carbon 13 and Proton Nuclear Magnetic Resonance
Morrow J, Keim P, Gurd F. CO2 Adducts of Certain Amino Acids, Peptides, and Sperm Whale Myoglobin Studied by Carbon 13 and Proton Nuclear Magnetic Resonance. Journal Of Biological Chemistry 1974, 249: 7484-7494. PMID: 4436319, DOI: 10.1016/s0021-9258(19)81264-4.Peer-Reviewed Original ResearchConceptsNuclear magnetic resonanceAmino acidsProton nuclear magnetic resonanceDeuterium isotope effectChemical shiftsCO2 adductCertain amino acidsSperm whale myoglobinNMR measurementsMagnetic resonanceCarbon-13Fast exchangeMost amino acidsEquilibrium constantsCarbamino adductsIsotope effectWhale myoglobinStructural consequencesAdductsAcidPeptidesAccurate determinationNMRResonanceSensitive functionLigand-dependent aggregation of chicken hemoglobin AI
Morrow J, Wittebort R, Gurd F. Ligand-dependent aggregation of chicken hemoglobin AI. Biochemical And Biophysical Research Communications 1974, 60: 1058-1065. PMID: 4429560, DOI: 10.1016/0006-291x(74)90420-3.Peer-Reviewed Original Research13C NMR Studies of the Interaction of Hb and Carbonic Anhydrase with 13CO2
Gurd F, Morrow J, Keim P, Visscher R, Marshall R. 13C NMR Studies of the Interaction of Hb and Carbonic Anhydrase with 13CO2. Advances In Experimental Medicine And Biology 1974, 48: 109-124. PMID: 4215298, DOI: 10.1007/978-1-4684-0943-7_6.Peer-Reviewed Original ResearchConceptsMetal-protein interactionsInteraction of CO2NMR studiesHydrated derivativeNMR spectrometerSmall moleculesInteraction of HbCarbonate saltsBuffer componentsBicarbonate ionsCarbonic anhydraseCO2NMRUnquestionable importanceCommon strategySpeciesProteinIonsInsolubilityMoleculesSaltInteractionDerivativesBicarbonateSpectrometer
1973
Interaction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations
Morrow J, Keim P, Visscher R, Marshall R, Gurd F. Interaction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations. Proceedings Of The National Academy Of Sciences Of The United States Of America 1973, 70: 1414-1418. PMID: 4514311, PMCID: PMC433509, DOI: 10.1073/pnas.70.5.1414.Peer-Reviewed Original Research