Letter from Linus Pauling to Allan Butler. January 19, 1950. Page 1  Larger Images / More Information. 1 p.  View Transcript

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Activity Listings

• Bill from the Southern Counties Gas Company of California to LP for $26.16. [Filed under LP Biographical: Business and Financial: (Assorted Bills, Receipts and Invoices, 1945-1950.), Box #4.059, Folder #59.3]
• Bill from the Union Oil Company of California to LP for $29.30. Series of bills from December,1949 and January,1950 attached. [Filed under LP Biographical: Business and Financial: (Assorted Bills, Receipts and Invoices, 1945-1950.), Box #4.059, Folder #59.3]
• Details of the Meetings of the Professorial Staff of the Division of Chemistry and Chemical Engineering on January 18th and 20th. [Filed under LP Biographical: Academia: (CIT: Materials re: Division of Chemistry and Chemical Engineering, 1946-1956.), Box #1.020, Folder #20.5]
• Letter from Emil Ott, Chairman, Committee on Financing of ACS Publications, American Chemical Society, to Professor M. S. Kharasch, University of Chicago, cc. LP RE: States that copies of his letter are being distributed to the committee and they agreed with the general ideas presented in his letter. States that the committee does not feel that his suggested way to raise funds is feasible but that they are looking into two alternate methods. [Letter from Kharasch and Reinmuth to the Editor January 17, 1950] [Filed under LP Correspondence: (Chemical Abstracts), #70.2]
• Letter from F. E. Simon, Clarendon Laboratory, Oxford, to LP RE: Discusses the difficulties that surround the engineering profession in England and the ideal solution to the problem would be to build Institutes for Technology at the same place as the university. Informs LP of their work on helium and the specific heats of rare earth metals. [Letters from LP to Simon January 11, 1950 and January 30, 1950] [Filed under LP Correspondence: (Simon, F. E.), #365.2]
• Letter from Jack McElhiney to LP RE: Encloses a copy of the Summary of Findings by the Board of Review of the Long Beach Naval Shipyard. Asks LP for a statement of his opinion concerning the report. Mentions his difficulty finding a job because his experience is so specialized. [Filed under LP Correspondence: (M: Correspondence, 1950), #256.1]
• Letter from L.W. Butz, Head, Chemistry Branch, Office of Naval Research to LP RE: Invites him to be the chairman of a committee designed to review proposals for scientific research sent to ONR for funding. Explains that ONR wants to make sure the research they are supporting is helping the science world. [Letter from LP to Butz January 30, 1950] [Filed under LP Science: (Office of Naval Research: Correspondence, Contract Status Reports and Project Status Reports, 1947-1962), Box #14.031, Folder #31.3]
• Letter from LP to Alden H. Emery, Executive Secretary, American Chemical Society RE: Nominates W.F. Giauque for the Priestley Medal and includes his “vita.” Includes a copy of the information that LP wrote about him. [Letter from Emery to Priestley Medal Committee January 4, 1950, letter from Emery to Priestley Medal Committee January 25, 1950] [Filed under LP Science: (American Chemical Society: Materials re: Committees and Awards, 1948-1951, 1967), Box #14.010, Folder #10.6]
• Letter from LP to Florence S. Chesse RE: Thanks her for the suggestion of having a footnote at the beginning of Chapter 5 and agrees that such a footnotes should be added. [Letter from Chesse to LP January 16, 1950] [Filed under LP Books: 1950b.2]
• Letter from LP to Harvey A. Itano, National Institute of Health. [Filed under LP Correspondence: (Itano, Harvey A.), #181.5]

  Dr. Itano Linus Pauling Jan. 20, 1950

  Nature of sickle cell hemoglobin

  I think that sickle cell hemoglobin and normal human hemoglobin represent two ways of coiling the polypeptide chain characteristic of hemoglobin molecule, and that these two ways are rather stable, being the two stable configurations of the molecule. This is, of course, the globin molecule.

  The evidence available so far indicates the difference in isoelectric point is not the result of a difference in amino acid composition of the globin. How, it has been reported, that when hemoglobin is denatured and renatured, it may occur in either one of two forms, differing in isoelectric point by 1.2 pH units. I think that these two forms correspond to normal human hemoglobin and sickle ceil anemia hemoglobin. Would you look up the article by Gralen and tell me what the isoelectric points are that he reported for the two forms.

  I believe that we should repeat Gralen's work, and see if we can prove this point.

  Moreover, I think that the two peaks which appear in your electrophoretic patterns of globin, both normal globin and sickle cell anemia globin, correspond to these two configurations. If we assume that the isoelectric point of globin is about the same as that of hemoglobin, 7 or a little less, and draw straight lines on a plot of mobility against pH to intersect the pH axis, the two lines passing through the observed mobilities for the slow components and the fast components in acetate buffer, at pH 4.64, we find that the intercepts differ by 0.23 pH units. The phosphate points do not give this result, the mobilities of the two components being reported

  Dr. Itano -2- 1/20/50

  as differing very little. I think that this may be due to a tendency of one of the globins to find phosphate preferentially, thus changing its charge. The place where the phosphate is bound is presumably the same place where I believe that heme is bound because I believe that you found that there was the same difference between sickle cell anemia hemoglobin and normal hemoglobin in phosphate buffer as in other buffer.

  It seems to me that your experiments with globin, showing that the same globin comes from normal hemoglobin and sickle cell hemoglobin, is pretty good evidence for our point. I think that to repeat Gralen's experiment with the two hemoglobins would just about clinch the matter. Would you talk with me about making plans to have this work carried out?

  It seems to me that one thing that we should consider is the possibility of converting one hemoglobin into the other simply by gentle heating, for a long time, at a temperature below the denaturation temperature. I suggest that we try the effect of heating both normal hemoglobin and sickle cell hemoglobin for several days, say, at a temperature of 58 °C, and then making electrophoretic patterns.

  Linus Pauling:W

• Letter from LP to Margherita Minchilli, Universita Adriatica (Italy), RE: States that he was interested to learn that she would like to translate General Chemistry into Italian and tells her that he has forwarded her letter to the publisher. Handwritten Note: “Letter sent to W. H. Freeman.” [Letter from Freeman to Minchilli January 26, 1950] [Filed under LP Books: 1947b6.2]
• Letter from LP to Mr. Arnold Nevis, Harvard Medical School Student, RE: Explains that he does not think that Nevis’ ideas are correct and that does not know of any experiments that would effectively prove Nevis’ hypotheses. [Letters from Nevis to LP December 2, 1949 and February 12, 1950] [Filed under LP Correspondence: (N: Correspondence, 1950), #287.17]
• Letter from Ricardo Carvallio Ferreira to LP RE: Congratulates LP on his recent paper, “Sickle Cell Anemia, a Molecular Disease,” which appeared in Science, November 25, 1949. Asks LP to send some of his recent reprints. [Filed under LP Correspondence: (Ferreira, Ricardo), #119.7]
• Pamphlet: “Methyl Green-Pyronin” by N. B. Kurnick and A. E. Mirsky. Reprinted from the Journal of General Physiology. [Filed under LP Science: (Non-Pauling Reprints re: The Structure and Properties of Proteins, 1920s - 1970s Box #6.006, Folder #6.1]
• Statement from George M. Stambach to AHP: Bills her for $63.28. [Filed under LP Biographical: Business and Financial: (Assorted Bills, Receipts and Invoices, 1945-1950.), Box #4.059, Folder #59.3]