Hemoglobins, Part C: Biophysical Methods: Volume 232
Published on 24. May 1994
Book
Hardback
725 pages
978-0-12-182133-3 (ISBN)
Description
Hemoglobin has been involved in the most significant advances in our understanding of modern genetics and molecular biology. Now, hemoglobin is again central to a new area: Development of artificial blood (blood substitute.)This volume of Methods in Enzymology and its companion Volume 231 are indispensable to anyone with a serious interest in this emerging field. They completely updated and extended the information presented in Volume 76, which was published more than 10 years ago.
Reviews / Votes
Praise for the Series"The Methods in Enzymology series represents the gold-standard."
--NEUROSCIENCE
"Incomparably useful."
--ANALYTICAL BIOCHEMISTRY
"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page."
--BIO/TECHNOLOGY
"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection."
--CHEMISTRY IN INDUSTRY
"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced."
--AMERICAN SOCIETY OF MICROBIOLOGY NEWS
"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work."
--ENZYMOLOGIA
"A series that has established itself as a definitive reference for biochemists."
--JOURNAL OF CHROMATOGRAPHY
More details
Series
Language
English
Place of publication
San Diego
United States
Publishing group
Elsevier Science Publishing Co Inc
Target group
Professional and scholarly
Biochemists, molecular biologists, cell biologists, physiologists, pathologists, biophysicists, clinical chemists, industrial and academic researchers involved in the preparation of hemoglobin derivatives and in the preparationand analysis of recombinant proteins.
Dimensions
Height: 229 mm
Width: 152 mm
Weight
1140 gr
ISBN-13
978-0-12-182133-3 (9780121821333)
Copyright in bibliographic data is held by Nielsen Book Services Limited or its licensors: all rights reserved.
Schweitzer Classification
Persons
Volume editor
School of Medicine, Texas Tech University Health Science Center, Lubbock, U.S.A.
University of California, Department of Medicine and Veterans Affairs Medical Center, San Diego, U.S.A.
Editor-in-chief
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
Content
Molecular Structure and Dynamics:
Y. Goto and A.L. Fink, Acid-Induced Folding of Heme Proteins.
R. Liddington, X-Ray Crystallography of Partially Liganded Structures.
S.W. Englander and J.J. Englander, Structure and Energy Change in Hemoglobin by Hydrogen Exchange Labeling.
S. Pin and C.A. Royer, High-Pressure Fluorescence Methods for Observing Subunit Dissociation in Hemoglobin.
A. Bellelli and M. Brunori, Optical Measurements of QuaternaryStructural Changes in Hemoglobin.
M.C. Marden, J. Kister, and C. Poyart, Allosteric Equilibirum Measurements with Hemoglobin Valency Hybrids.
G. McLendon and J. Feitelson,Electron-Transfer Reactions of Hemoglobin with Small Molecules: A Potential Probe of Conformational Dynamics. Spectroscopy:
C. Ho and J.R. Perussi, Proton Nuclear Magnetic Resonance Studies of Hemoglobin.
A. Dong and W.S. Caughey, Infrared Methods for Study of Hemoglobin Reactions and Structures.
R. H. Austin and L. J. Rothberg, Picosecond Infrared Spectroscopy of Hemoglobin and Myoglobin.
J.M. Friedman, Time-Resolved Resonance Raman Spectroscopy as Probe of Structure, Dynamics, and Reactivity in Hemoglobin.
R.E. Hirsch, Front-Face Fluorescence Spectroscopy of Hemoglobins.
C. Zentz, S. Pin, and B. Alpert, Stationary and Time-Resolved Circular Dichroism of Hemoglobins.
S. Pin, B. Alpert, A. Congiu-Castellano, S.D. Longa, and A. Bianconi, X-Ray Absorption Spectroscopy of Hemoglobin.
F.A. Ferrone, Modulated Excitation Spectroscopy in Hemoglobin.
J. Deak, L. Richard, M. Pereira, H.-L. Chui, and R.J.D. Miller, Picosecond Phase Grating Spectroscopy: Applications to Bioenergetics and Protein Dynamics.
Ligand Binding:
A.J. Mathews and J.S. Olson, Assignment of Rate Constants for O2 and CO Binding to a and b Subunits within R- and T-State Human Hemoglobin.
J. Hofrichter, A. Ansari, C.M. Jones, R.M. Deutsch, J.H. Sommer, and E.R. Henry, Ligand Binding and Conformational Changes Measured by Time-Resolved Absorption Spectroscopy.
J.-L. Martin and M.H. Vos, Femtosecond Measurements of Geminate Recombination in Heme Proteins.
V.S. Sharma, Double Mixing Methods for Kinetic Studies of Ligand Binding inPartially Liganded Intermediates of Hemoglobin.
M. Perrella and L. Rossi-Bernardi, Hemoglobin-Liganded Intermediates.
K.D. Vandegriff and R.I. Shrager, Hemoglobin-Oxygen Equilibrium Binding: Rapid-Scanning Spectrophotometry and Singular Value Decomposition.
R.M. Winslow, A. Murray, and C.C. Gibson, Oxygen Equilibrium Curve of Concentrated Hemoglobin.
C. Poyart, M.C. Marden, and J. Kister, Bezafibrate Derivatives as Potent Effectors of Hemoglobin.
Mathematical Analysis and Modeling:
R.L. Berger, N. Davids, and M. Perrella, Simulation of Hemoglobin Kinetics Using Finite Element Numerical Methods.
K. Imai, Adair Fitting to Oxygen Equilibrium Curves of Hemoglobin.
M.L. Doyle, D.W. Myers, G.K. Ackers, and R. I. Shrager, Weighted Nonlinear Regression Analysis of Highly Cooperative Oxygen Equilibrium Curves.
M.L. Johnson, Dimer-Tetramer Equilibrium in Adair Fitting.
L. J. Parkhurst, T.M. Larsen, and H.-Y. Lee, Effects of Wavelength on Fitting Adair Constants for Binding of Oxygen to Human Hemoglobin.
E.C. DeLand, Adair Equation: Rederiving Oxygenation Parameters.
E. Di Cera, Linkage Thermodynamics.
Author Index.
Subject Index.
Y. Goto and A.L. Fink, Acid-Induced Folding of Heme Proteins.
R. Liddington, X-Ray Crystallography of Partially Liganded Structures.
S.W. Englander and J.J. Englander, Structure and Energy Change in Hemoglobin by Hydrogen Exchange Labeling.
S. Pin and C.A. Royer, High-Pressure Fluorescence Methods for Observing Subunit Dissociation in Hemoglobin.
A. Bellelli and M. Brunori, Optical Measurements of QuaternaryStructural Changes in Hemoglobin.
M.C. Marden, J. Kister, and C. Poyart, Allosteric Equilibirum Measurements with Hemoglobin Valency Hybrids.
G. McLendon and J. Feitelson,Electron-Transfer Reactions of Hemoglobin with Small Molecules: A Potential Probe of Conformational Dynamics. Spectroscopy:
C. Ho and J.R. Perussi, Proton Nuclear Magnetic Resonance Studies of Hemoglobin.
A. Dong and W.S. Caughey, Infrared Methods for Study of Hemoglobin Reactions and Structures.
R. H. Austin and L. J. Rothberg, Picosecond Infrared Spectroscopy of Hemoglobin and Myoglobin.
J.M. Friedman, Time-Resolved Resonance Raman Spectroscopy as Probe of Structure, Dynamics, and Reactivity in Hemoglobin.
R.E. Hirsch, Front-Face Fluorescence Spectroscopy of Hemoglobins.
C. Zentz, S. Pin, and B. Alpert, Stationary and Time-Resolved Circular Dichroism of Hemoglobins.
S. Pin, B. Alpert, A. Congiu-Castellano, S.D. Longa, and A. Bianconi, X-Ray Absorption Spectroscopy of Hemoglobin.
F.A. Ferrone, Modulated Excitation Spectroscopy in Hemoglobin.
J. Deak, L. Richard, M. Pereira, H.-L. Chui, and R.J.D. Miller, Picosecond Phase Grating Spectroscopy: Applications to Bioenergetics and Protein Dynamics.
Ligand Binding:
A.J. Mathews and J.S. Olson, Assignment of Rate Constants for O2 and CO Binding to a and b Subunits within R- and T-State Human Hemoglobin.
J. Hofrichter, A. Ansari, C.M. Jones, R.M. Deutsch, J.H. Sommer, and E.R. Henry, Ligand Binding and Conformational Changes Measured by Time-Resolved Absorption Spectroscopy.
J.-L. Martin and M.H. Vos, Femtosecond Measurements of Geminate Recombination in Heme Proteins.
V.S. Sharma, Double Mixing Methods for Kinetic Studies of Ligand Binding inPartially Liganded Intermediates of Hemoglobin.
M. Perrella and L. Rossi-Bernardi, Hemoglobin-Liganded Intermediates.
K.D. Vandegriff and R.I. Shrager, Hemoglobin-Oxygen Equilibrium Binding: Rapid-Scanning Spectrophotometry and Singular Value Decomposition.
R.M. Winslow, A. Murray, and C.C. Gibson, Oxygen Equilibrium Curve of Concentrated Hemoglobin.
C. Poyart, M.C. Marden, and J. Kister, Bezafibrate Derivatives as Potent Effectors of Hemoglobin.
Mathematical Analysis and Modeling:
R.L. Berger, N. Davids, and M. Perrella, Simulation of Hemoglobin Kinetics Using Finite Element Numerical Methods.
K. Imai, Adair Fitting to Oxygen Equilibrium Curves of Hemoglobin.
M.L. Doyle, D.W. Myers, G.K. Ackers, and R. I. Shrager, Weighted Nonlinear Regression Analysis of Highly Cooperative Oxygen Equilibrium Curves.
M.L. Johnson, Dimer-Tetramer Equilibrium in Adair Fitting.
L. J. Parkhurst, T.M. Larsen, and H.-Y. Lee, Effects of Wavelength on Fitting Adair Constants for Binding of Oxygen to Human Hemoglobin.
E.C. DeLand, Adair Equation: Rederiving Oxygenation Parameters.
E. Di Cera, Linkage Thermodynamics.
Author Index.
Subject Index.