Hemoglobin Disorders: Molecular Methods and Protocols 2003 Edition Contributor(s): Nagel, Ronald L. (Editor) |
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ISBN: 0896039625 ISBN-13: 9780896039629 Publisher: Humana OUR PRICE: $104.49 Product Type: Hardcover - Other Formats Published: March 2003 Annotation: A collection of readily reproducible experimental and clinical techniques for studying the molecular basis of hemoglobin disorders. These step-by-step methods utilize a wide variety of the latest analytical techniques, including x-ray crystallography, high performance liquid chromatography, electrophoresis, and nuclear magnetic resonance. Additional methods are offered for prenatal diagnostic analysis, the DNA diagnosis of hemoglobin mutations, hemoglobin fluorescence, and the semisynthesis of hemoglobin. |
Additional Information |
BISAC Categories: - Medical | Hematology - Medical | Laboratory Medicine |
Dewey: 616.151 |
LCCN: 2003040674 |
Series: Methods in Molecular Medicine |
Physical Information: 1.1" H x 6.06" W x 9.52" (1.72 lbs) 300 pages |
Descriptions, Reviews, Etc. |
Publisher Description: Hemoglobin and Hemoglobinologists This volume, Hemoglobin Disorders: Molecular Methods and Protocols, will be introduced with a review of the great milestones in the field, and the scientists responsible for those achievements. The history of hemoglobin can be divided into three periods: the Classical period, the Modern period, and the Post-Modern period. I am inclined to include as the four major members of the classical period Francis Roughton, Quentin Gibson, Jeffries Wyman, and Linus Pauling, not only because of their achievements, but also because of the superb scientists they trained and/or influenced. Francis John Worsely Roughton (1899-1972) (Fig. 1), in his laboratory at Trinity College in Cambridge, England, made the first measurements of the rapid reaction of oxygen with hemoglobin at the millisecond scale, at first by flow-mixing methods and later by flash photolysis. He not only opened an era of molecular research of hemoglobin, but also invented the methodology for fast reactions through the use of laser technology, which was later improved by others so that even faster reactions could be detected. Another contribution of Roughton was the education of Quentin H. Gibson (Fig. 2), his favorite s- dent, who, in his laboratory in Sheffield, continued to expand the horizon of ligand binding to hemoglobin, defining the oxygen binding constants for each of the hemes of hemoglobin. Though this did not, as expected, solve the und- lying mechanism of ligand cooperativity as discussed below, it was nonet- less an important milestone. |