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Blood and tissue oxygen carriers / guest editor: Ch. P. Mangum ; with contributions by M. Brouwer ... [et al.]
Blood and tissue oxygen carriers / guest editor: Ch. P. Mangum ; with contributions by M. Brouwer ... [et al.]
Pubbl/distr/stampa Berlin ; New York : Springer-Verlag, c1992
Descrizione fisica xviii, 459 p. : ill ; 25 cm
Altri autori (Persone) Mangum, Charlotte P.author
Brouwer, Marius
Collana Advances in comparative and environmental physiology ; 13
Soggetto topico Hemoglobin
Hemocyanin
Oxygen - Physiological transport
ISBN 3540536574
Classificazione LC QP33.38
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Record Nr. UNISALENTO-991001508749707536
Berlin ; New York : Springer-Verlag, c1992
Materiale a stampa
Lo trovi qui: Univ. del Salento
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Hemoglobin-based oxygen carriers as red cell substitutes and oxygen therapeutics / / Hae Won Kim, A. Gerson Greenburg, editors
Hemoglobin-based oxygen carriers as red cell substitutes and oxygen therapeutics / / Hae Won Kim, A. Gerson Greenburg, editors
Edizione [1st ed. 2013.]
Pubbl/distr/stampa Heidelberg [Germany] : , : Springer, , 2013
Descrizione fisica 1 online resource (xxiii, 746 pages) : illustrations (some color)
Disciplina 611.01816
615.19
615.399
616.15
Collana Gale eBooks
Soggetto topico Oxygen - Physiological transport
Oxygen therapy
Blood substitutes
ISBN 3-642-40717-X
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Brief historical account of HBOC development -- Physiology of respiration -- Oxygen transport to tissues -- Pathophysiology of acute anemia -- Global blood safety and need for safe blood supply -- Blood transfusion and its limitations -- Scientific basis and design of HBOCs -- HBOCs: a regulatory perspective -- Current HBOC products in development -- Clinical indications and clinical trials of HBOCs -- HBOCs and adverse events observed in clinical trials -- HBOC-mediated vasoactivity and hypertension -- HBOC and oxygen and nitrogen radical mediated toxicity -- HBOCs and clinical laboratory interference -- Animal models for HBOC studies -- New emerging Technologies for universal RBCs -- Future prospects.
Record Nr. UNINA-9910437798003321
Heidelberg [Germany] : , : Springer, , 2013
Materiale a stampa
Lo trovi qui: Univ. Federico II
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Recent advances in microbial oxygen-binding proteins / / [edited by] Robert K. Poole, West Riding Professor of Microbiology, Department of Molecular Biology and Biotechnology, the University of Sheffield, Firth Court, Western Bank, Sheffield, UK
Recent advances in microbial oxygen-binding proteins / / [edited by] Robert K. Poole, West Riding Professor of Microbiology, Department of Molecular Biology and Biotechnology, the University of Sheffield, Firth Court, Western Bank, Sheffield, UK
Edizione [First edition.]
Pubbl/distr/stampa Amsterdam : , : Elsevier, , 2015
Descrizione fisica 1 online resource (372 p.)
Collana Advances in microbial physiology
Soggetto topico Microorganisms - Physiology
Oxygen - Physiological transport
Soggetto genere / forma Electronic books.
ISBN 0-12-803332-0
0-12-803298-7
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Front Cover; Recent Advances in Microbial Oxygen-Binding Proteins; Copyright; Contents; Contributors; Preface; Acknowledgement; Chapter One: Cytochromes cʹ: Structure, Reactivity and Relevance to Haem-Based Gas Sensing; 1. Introduction; 2. Occurrence; 3. Proposed Functional Roles of Cytochromes c'; 4. Structural Properties of Cytochromes c'; 4.1. Oligomeric State and Solvent Channels; 4.1.1. Dimer Arrangements and Monomerization; 4.1.2. Solvent Accessible Channels Between the Protein Surface and the Haem Pockets; 4.2. Haem Environment (in the Absence of Exogenous Ligands)
4.2.1. Structure of the Distal Pocket4.2.2. Structure of the Proximal Haem Pocket; 4.2.3. Redox State-Dependent Changes to the Haem Environment; 4.3. Crystal Structures of Ligand-Bound Forms; 4.3.1. Alkylisocyanide Binding to RCCP; 4.3.2. CO- and NO-Bound Structures of AXCP and SFCP; 5. Spectroscopic Properties of Cytochromes cʹ; 5.1. Haem Spectroscopy in the Absence of Exogenous Ligands; 5.1.1. Ferric Cytochromes c'; 5.1.2. Ferrous Cytochromes c'; 5.1.3. Four-Coordinate Cytochrome c'; 5.2. Haem Spectroscopy of Cytochromes cʹ with Exogenous Ligands; 5.2.1. Ferrous Complexes with NO
5.2.2. Ferrous Complexes with Carbon Monoxide5.2.3. Ferrous Complexes with Dioxygen; 5.2.4. Ferrous Complexes with Alkyl Isocyanides; 5.2.5. Ferric Complexes with Exogenous Ligands; 6. Structure-Reactivity Relationships in Cytochromes cʹ; 6.1. Distal Haem Coordination; 6.1.1. Reactivity of Cytochromes cʹ with Diatomic Gases; 6.1.1.1. Ferrous 6cXO Complexes (X=N, C, O); 6.1.1.2. Structural Determinants of Distal kon Values; 6.1.1.3. Structural Determinants of Distal koff Values; 6.1.1.4. Ligand-Induced Dimer Dissociation; 6.1.1.5. 6cNO Complexes of Ferric Cytochromes c
6.1.2. Reactivity of Cytochromes cʹ with Bulky Distal Ligands6.1.2.1. Alkyl Isocyanides; 6.1.2.2. Imidazole; 6.1.3. Reactivity of Cytochromes cʹ with Anionic Distal Ligands; 6.1.4. Conformational Control of Distal Ligand Binding in SFCP; 6.2. Proximal 5cNO Formation; 6.2.1. Determinants of Proximal 5cNO Formation; 6.2.1.1. FeHis Bond Scission; 6.2.1.2. Rapid Proximal NO Binding; 6.2.1.3. Steric Hindrance of Distal NO Binding; 6.2.1.4. Stability of the Proximal 5cNO Complex; 6.2.1.5. Long-Range Effects; 7. Relevance of Cytochrome cʹ to Other Proteins, Including Haem-Based Gas Sensors
AcknowledgementsReferences; Chapter Two: Bridging Theory and Experiment to Address Structural Properties of Truncated Haemoglobins: Insights from The...; 1. Introduction; 1.1. Microbial Haemoglobins; 1.2. Truncated Haemoglobins; 2. An Overview of Resonance Raman Spectroscopy of Haem Proteins; 2.1. Core-Size Marker Bands; 2.2. Fe-Ligand Modes; 2.2.1. The Proximal Iron-Histidine Stretching Mode; 2.2.2. The Distal Ligands; 2.2.2.1. H2O/OH-; 2.2.2.2. Fluoride; 2.2.2.3. H2S; 2.2.2.4. O2; 2.2.2.5. CO; 3. Computer Simulation Techniques; 4. Thermobifida fusca Hb; 4.1. Haem Cavity Structure
5. Spectroscopy and Computer Simulation of Tf-trHb
Record Nr. UNINA-9910461009903321
Amsterdam : , : Elsevier, , 2015
Materiale a stampa
Lo trovi qui: Univ. Federico II
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Recent advances in microbial oxygen-binding proteins / / [edited by] Robert K. Poole, West Riding Professor of Microbiology, Department of Molecular Biology and Biotechnology, the University of Sheffield, Firth Court, Western Bank, Sheffield, UK
Recent advances in microbial oxygen-binding proteins / / [edited by] Robert K. Poole, West Riding Professor of Microbiology, Department of Molecular Biology and Biotechnology, the University of Sheffield, Firth Court, Western Bank, Sheffield, UK
Edizione [First edition.]
Pubbl/distr/stampa Amsterdam : , : Elsevier, , 2015
Descrizione fisica 1 online resource (372 p.)
Collana Advances in microbial physiology
Soggetto topico Microorganisms - Physiology
Oxygen - Physiological transport
ISBN 0-12-803332-0
0-12-803298-7
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Front Cover; Recent Advances in Microbial Oxygen-Binding Proteins; Copyright; Contents; Contributors; Preface; Acknowledgement; Chapter One: Cytochromes cʹ: Structure, Reactivity and Relevance to Haem-Based Gas Sensing; 1. Introduction; 2. Occurrence; 3. Proposed Functional Roles of Cytochromes c'; 4. Structural Properties of Cytochromes c'; 4.1. Oligomeric State and Solvent Channels; 4.1.1. Dimer Arrangements and Monomerization; 4.1.2. Solvent Accessible Channels Between the Protein Surface and the Haem Pockets; 4.2. Haem Environment (in the Absence of Exogenous Ligands)
4.2.1. Structure of the Distal Pocket4.2.2. Structure of the Proximal Haem Pocket; 4.2.3. Redox State-Dependent Changes to the Haem Environment; 4.3. Crystal Structures of Ligand-Bound Forms; 4.3.1. Alkylisocyanide Binding to RCCP; 4.3.2. CO- and NO-Bound Structures of AXCP and SFCP; 5. Spectroscopic Properties of Cytochromes cʹ; 5.1. Haem Spectroscopy in the Absence of Exogenous Ligands; 5.1.1. Ferric Cytochromes c'; 5.1.2. Ferrous Cytochromes c'; 5.1.3. Four-Coordinate Cytochrome c'; 5.2. Haem Spectroscopy of Cytochromes cʹ with Exogenous Ligands; 5.2.1. Ferrous Complexes with NO
5.2.2. Ferrous Complexes with Carbon Monoxide5.2.3. Ferrous Complexes with Dioxygen; 5.2.4. Ferrous Complexes with Alkyl Isocyanides; 5.2.5. Ferric Complexes with Exogenous Ligands; 6. Structure-Reactivity Relationships in Cytochromes cʹ; 6.1. Distal Haem Coordination; 6.1.1. Reactivity of Cytochromes cʹ with Diatomic Gases; 6.1.1.1. Ferrous 6cXO Complexes (X=N, C, O); 6.1.1.2. Structural Determinants of Distal kon Values; 6.1.1.3. Structural Determinants of Distal koff Values; 6.1.1.4. Ligand-Induced Dimer Dissociation; 6.1.1.5. 6cNO Complexes of Ferric Cytochromes c
6.1.2. Reactivity of Cytochromes cʹ with Bulky Distal Ligands6.1.2.1. Alkyl Isocyanides; 6.1.2.2. Imidazole; 6.1.3. Reactivity of Cytochromes cʹ with Anionic Distal Ligands; 6.1.4. Conformational Control of Distal Ligand Binding in SFCP; 6.2. Proximal 5cNO Formation; 6.2.1. Determinants of Proximal 5cNO Formation; 6.2.1.1. FeHis Bond Scission; 6.2.1.2. Rapid Proximal NO Binding; 6.2.1.3. Steric Hindrance of Distal NO Binding; 6.2.1.4. Stability of the Proximal 5cNO Complex; 6.2.1.5. Long-Range Effects; 7. Relevance of Cytochrome cʹ to Other Proteins, Including Haem-Based Gas Sensors
AcknowledgementsReferences; Chapter Two: Bridging Theory and Experiment to Address Structural Properties of Truncated Haemoglobins: Insights from The...; 1. Introduction; 1.1. Microbial Haemoglobins; 1.2. Truncated Haemoglobins; 2. An Overview of Resonance Raman Spectroscopy of Haem Proteins; 2.1. Core-Size Marker Bands; 2.2. Fe-Ligand Modes; 2.2.1. The Proximal Iron-Histidine Stretching Mode; 2.2.2. The Distal Ligands; 2.2.2.1. H2O/OH-; 2.2.2.2. Fluoride; 2.2.2.3. H2S; 2.2.2.4. O2; 2.2.2.5. CO; 3. Computer Simulation Techniques; 4. Thermobifida fusca Hb; 4.1. Haem Cavity Structure
5. Spectroscopy and Computer Simulation of Tf-trHb
Record Nr. UNINA-9910797743203321
Amsterdam : , : Elsevier, , 2015
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Recent advances in microbial oxygen-binding proteins / / [edited by] Robert K. Poole, West Riding Professor of Microbiology, Department of Molecular Biology and Biotechnology, the University of Sheffield, Firth Court, Western Bank, Sheffield, UK
Recent advances in microbial oxygen-binding proteins / / [edited by] Robert K. Poole, West Riding Professor of Microbiology, Department of Molecular Biology and Biotechnology, the University of Sheffield, Firth Court, Western Bank, Sheffield, UK
Edizione [First edition.]
Pubbl/distr/stampa Amsterdam : , : Elsevier, , 2015
Descrizione fisica 1 online resource (372 p.)
Collana Advances in microbial physiology
Soggetto topico Microorganisms - Physiology
Oxygen - Physiological transport
ISBN 0-12-803332-0
0-12-803298-7
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Front Cover; Recent Advances in Microbial Oxygen-Binding Proteins; Copyright; Contents; Contributors; Preface; Acknowledgement; Chapter One: Cytochromes cʹ: Structure, Reactivity and Relevance to Haem-Based Gas Sensing; 1. Introduction; 2. Occurrence; 3. Proposed Functional Roles of Cytochromes c'; 4. Structural Properties of Cytochromes c'; 4.1. Oligomeric State and Solvent Channels; 4.1.1. Dimer Arrangements and Monomerization; 4.1.2. Solvent Accessible Channels Between the Protein Surface and the Haem Pockets; 4.2. Haem Environment (in the Absence of Exogenous Ligands)
4.2.1. Structure of the Distal Pocket4.2.2. Structure of the Proximal Haem Pocket; 4.2.3. Redox State-Dependent Changes to the Haem Environment; 4.3. Crystal Structures of Ligand-Bound Forms; 4.3.1. Alkylisocyanide Binding to RCCP; 4.3.2. CO- and NO-Bound Structures of AXCP and SFCP; 5. Spectroscopic Properties of Cytochromes cʹ; 5.1. Haem Spectroscopy in the Absence of Exogenous Ligands; 5.1.1. Ferric Cytochromes c'; 5.1.2. Ferrous Cytochromes c'; 5.1.3. Four-Coordinate Cytochrome c'; 5.2. Haem Spectroscopy of Cytochromes cʹ with Exogenous Ligands; 5.2.1. Ferrous Complexes with NO
5.2.2. Ferrous Complexes with Carbon Monoxide5.2.3. Ferrous Complexes with Dioxygen; 5.2.4. Ferrous Complexes with Alkyl Isocyanides; 5.2.5. Ferric Complexes with Exogenous Ligands; 6. Structure-Reactivity Relationships in Cytochromes cʹ; 6.1. Distal Haem Coordination; 6.1.1. Reactivity of Cytochromes cʹ with Diatomic Gases; 6.1.1.1. Ferrous 6cXO Complexes (X=N, C, O); 6.1.1.2. Structural Determinants of Distal kon Values; 6.1.1.3. Structural Determinants of Distal koff Values; 6.1.1.4. Ligand-Induced Dimer Dissociation; 6.1.1.5. 6cNO Complexes of Ferric Cytochromes c
6.1.2. Reactivity of Cytochromes cʹ with Bulky Distal Ligands6.1.2.1. Alkyl Isocyanides; 6.1.2.2. Imidazole; 6.1.3. Reactivity of Cytochromes cʹ with Anionic Distal Ligands; 6.1.4. Conformational Control of Distal Ligand Binding in SFCP; 6.2. Proximal 5cNO Formation; 6.2.1. Determinants of Proximal 5cNO Formation; 6.2.1.1. FeHis Bond Scission; 6.2.1.2. Rapid Proximal NO Binding; 6.2.1.3. Steric Hindrance of Distal NO Binding; 6.2.1.4. Stability of the Proximal 5cNO Complex; 6.2.1.5. Long-Range Effects; 7. Relevance of Cytochrome cʹ to Other Proteins, Including Haem-Based Gas Sensors
AcknowledgementsReferences; Chapter Two: Bridging Theory and Experiment to Address Structural Properties of Truncated Haemoglobins: Insights from The...; 1. Introduction; 1.1. Microbial Haemoglobins; 1.2. Truncated Haemoglobins; 2. An Overview of Resonance Raman Spectroscopy of Haem Proteins; 2.1. Core-Size Marker Bands; 2.2. Fe-Ligand Modes; 2.2.1. The Proximal Iron-Histidine Stretching Mode; 2.2.2. The Distal Ligands; 2.2.2.1. H2O/OH-; 2.2.2.2. Fluoride; 2.2.2.3. H2S; 2.2.2.4. O2; 2.2.2.5. CO; 3. Computer Simulation Techniques; 4. Thermobifida fusca Hb; 4.1. Haem Cavity Structure
5. Spectroscopy and Computer Simulation of Tf-trHb
Record Nr. UNINA-9910809433103321
Amsterdam : , : Elsevier, , 2015
Materiale a stampa
Lo trovi qui: Univ. Federico II
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Der Sauerstoff-Status des arteriellen Blutes : 1. Interdisziplinäres Mainzer Symposium der Angewandten Physiologie und klinischen Anästhesiologie, Mainz, Oktober 1986 / / R. Zander
Der Sauerstoff-Status des arteriellen Blutes : 1. Interdisziplinäres Mainzer Symposium der Angewandten Physiologie und klinischen Anästhesiologie, Mainz, Oktober 1986 / / R. Zander
Autore Zander R.
Pubbl/distr/stampa Basel : , : S. Karger, , 1988
Descrizione fisica 1 online resource (xii, 315 pages)
Disciplina 616.2
Soggetto topico Oxygen - Physiological transport
ISBN 3-318-05401-1
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Altri titoli varianti Sauerstoff-Status des arteriellen Blutes
Record Nr. UNINA-9910153270403321
Zander R.  
Basel : , : S. Karger, , 1988
Materiale a stampa
Lo trovi qui: Univ. Federico II
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