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CONFERENCE ON HEMOGLOBIN 2-3 MAY 1957 (1958)
National Academy of Sciences (NAS)

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. "Discussion." CONFERENCE ON HEMOGLOBIN 2-3 MAY 1957. Washington, DC: The National Academies Press, 1958.

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Page
225
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Page
225
Front Matter (R1-R2)
Contents (R7-R13)
Preface (R3-R4)
Foreword (R5-R6)
Opening Remarks (R14-R14)
Part I. Structure of Hemoglobin: Current Concepts of Structure of Hemoglobin (1-13)
Individual Velocity Constants in the Chain of Reaction of Sheep Hemoglobin with Dissolved Gases (14-26)
Discussion (27-32)
A Survey of the Evidence For and Against a Crevice Configuration for the Heme in Hemoglobin (33-47)
Discussion (48-49)
X-Ray Analysis of Haemoglobin (50-60)
Discussion (61-65)
Part II. Biosynthesis of Hemoglobin: The Biosynthesis of Porphyrin (66-73)
The Enzymatic Synthesis of Uroporphyrinogens from Porphobilinogen (74-83)
Enzymatic Studies of Protoporphyrin Synthesis (84-91)
Discussion (92-94)
The Role of Iron in Hemoglobin Synthesis (95-99)
The Role of Copper in Erythropoiesis (100-109)
Discussion (110-110)
Hemoglobin Synthesis in Vitro in Rabbit Reticulocytes (111-129)
Discussion (130-130)
The Incorporation of Glycine into Globin and the Synthesis of Heme in Duck Erythrocytes and Rabbit Reticulocytes (131-139)
Discussion (140-143)
Part III. Abnormal Hemoglobins: Electrophoretic Analyses of Abnormal Human Hemoglobins (144-153)
Discussion (154-156)
Zone Electrophoresis and the Minor Hemoglobin Components of Normal Human Blood (157-161)
Discussion (162-164)
A Method for the Characterization of Abnormal Human Hemoglobins Based Upon Differences in Chromatographic Behavior on Amberlite IRC 50 (165-165)
Discussion (166-171)
The Alkali Denaturation Procedures (172-175)
Discussion (176-178)
Immunologic Aspects of the Human Hemoglobin (179-181)
Discussion (182-182)
Studies on the Heterogeneity of Adult and Fetal Hemoglobins by Salting-Out, Alkali Denaturation and Moving Boundary Electrophoresis (183-198)
Discussion (199-200)
Heterogeneity of Hemoglobin and Methods of Isotopic Biosynthesis (201-211)
Starch Electrophoresis of Hemoglobin: Findings in Thalessemia Syndrome (212-214)
Discussion (215-219)
Observations on the Amino Acid Composition of Human Hemoglobins (220-224)
Discussion (225-226)
The Structural Basis of Difference in Electrophoretic Behavior of Human Hemoglobins (227-231)
Discussion (232-232)
The Chemical Difference Between Normal Human and Sickle Cell Anaemia Haemoglobins (233-237)
Discussion (238-252)
Part IV. Genetic Aspects of Abnormal Hemoglobins: Genetic Aspects of Hemoglobin (253-271)
Discussion (272-275)
Part V. Clinical Characteristics Associated with Abnormal Hemoglobins: Clinical Manifestations of Sickle Cell Disease (276-282)
The Thalassemia Syndromes (283-286)
Hemoglobin C. Diseases (287-294)
Discussion (295-295)
Closing Remarks (296-296)
Attendance List (297-302)
Index of Authors and Discussions (303-304)

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OCR for page 226
226 PART III. ABNORMAL HEMOGLOBINS decrease under the same condition of hydrolysis. No increase is observed after ]5 minutes. There is very little DNP-valine after 15 minutes of hydrolysis, but thereafter it increases with continued hydrolysis more rapidly than DNP- valine is released from DNP-valyl-leucine. Because we know the rate at which DNP-valine is released from DNP-valyl-leucine, we can calculate the amount that must be coming from the other two chains that do not release DNP-valyl-leucine. When we do this, we find that the first order reaction rate constant is something like 0.70 hr.-i, whereas the constant for DNP- valyl-leucine itself is 0.143 hr.-~. The DNP-valine from the two chains other than those that release DNP-valyl-leucine is coming off more slowly. By cal- culation we find that in 22 hours of hydrolysis there still should remain ap- proximately 20 per cent of the two resistant chains unhydrolyzed. Since there are two chains, this is equivalent to 0.4 of an N-terminal group. Our previous value was 3.6 and the addition of 0.4 comes out so perfectly to 4.0 as to be almost unrealistic. There are a good many implications in these results that I don't have time to discuss. They certainly show, however, that there are two kinds of chains in the molecule. This work is described in an article scheduled for publication.) REFEREN CE 1. Rhinesmith, H. S., Schroeder, W. A., and Pauling, I.: N-terminal amino acid residues of normal adult human hemoglobin: A quantitative study of certain aspects of Sanger's dinitrophenyl (DNP) method, J. Am. Chem. Soc. 79: 609— 615, 1957.

Representative terms from entire chapter:

hemoglobins decrease