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. 1966 Mar;55(3):586–592. doi: 10.1073/pnas.55.3.586

The presence of two major hemoglobin components in an inbred strain of mice.

D B Rifkin, M R Rifkin, W Konigsberg
PMCID: PMC224192  PMID: 5221243

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BAGLIONI C. An improved method for the fingerprinting of human hemoglobin. Biochim Biophys Acta. 1961 Apr 1;48:392–396. doi: 10.1016/0006-3002(61)90490-5. [DOI] [PubMed] [Google Scholar]
  2. BARGETZI J. P., THOMPSON E. O., SAMPATHKUMAR K. S., WALSH K. A., NEURATH H. THE AMINO- AND CARBOXYL-TERMINAL RESIDUES AND THE SELF-DIGESTION OF BOVINE PANCREATIC CARBOXYPEPTIDASE A. J Biol Chem. 1964 Nov;239:3767–3774. [PubMed] [Google Scholar]
  3. BEAVEN G. H., HOLIDAY E. R. Ultraviolet absorption spectra of proteins and amino acids. Adv Protein Chem. 1952;7:319–386. doi: 10.1016/s0065-3233(08)60022-4. [DOI] [PubMed] [Google Scholar]
  4. HILL R. J., KONIGSBERG W., GUIDOTTI G., CRAIG L. C. The structure of human hemoglobin. I. The separation of the alpha and beta chains and their amino acid composition. J Biol Chem. 1962 May;237:1549–1554. [PubMed] [Google Scholar]
  5. HUTTON J. J., BISHOP J., SCHWEET R., RUSSELL E. S. Hemoglobin inheritance in inbred mouse strains. I. Structural differences. Proc Natl Acad Sci U S A. 1962 Sep 15;48:1505–1513. doi: 10.1073/pnas.48.9.1505. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. HUTTON J. J., SCHWEET R. S., WOLFE H. G., RUSSELL E. S. HEMOGLOBIN SOLUBILITY AND ALPHA-CHAIN STRUCTURE IN CROSSES BETWEEN TWO INBREAD MOUSE STRAINS. Science. 1964 Jan 17;143(3603):252–253. doi: 10.1126/science.143.3603.252. [DOI] [PubMed] [Google Scholar]
  7. INGRAM V. M. Gene evolution and the haemoglobins. Nature. 1961 Mar 4;189:704–708. doi: 10.1038/189704a0. [DOI] [PubMed] [Google Scholar]
  8. KONIGSBERG W., HILL R. J. The structure of human hemoglobin. III. The sequence of amino acids in the tryptic peptides of the alpha chain. J Biol Chem. 1962 Aug;237:2547–2561. [PubMed] [Google Scholar]
  9. MATSUBARA H., SMITH E. L. HUMAN HEART CYTOCHROME C. CHYMOTRYPTIC PEPTIDES, TRYPTIC PEPTIDES, AND THE COMPLETE AMINO ACID SEQUENCE. J Biol Chem. 1963 Aug;238:2732–2753. [PubMed] [Google Scholar]
  10. POPP R. A. Studies on the mouse hemoglobin loci. II. Position of the hemoglobin locus with respect to albinism and shaker-1 loci. J Hered. 1962 Mar-Apr;53:73–80. doi: 10.1093/oxfordjournals.jhered.a107127. [DOI] [PubMed] [Google Scholar]
  11. POPP R. A. THE SEPARATION AND AMINO ACID COMPOSITION OF THE TRYPTIC PEPTIDES OF THE ALPHA CHAIN OF HEMOGLOBIN FROM C57BL MICE. J Biol Chem. 1965 Jul;240:2863–2867. [PubMed] [Google Scholar]
  12. Popp R. A. Hemoglobin variants in mice. Fed Proc. 1965 Sep-Oct;24(5):1252–1257. [PubMed] [Google Scholar]
  13. WEISBLUM B., GONANO F., VON EHRENSTEIN, BENZER S. A DEMONSTRATION OF CODING DEGENERACY FOR LEUCINE IN THE SYNTHESIS OF PROTEIN. Proc Natl Acad Sci U S A. 1965 Feb;53:328–334. doi: 10.1073/pnas.53.2.328. [DOI] [PMC free article] [PubMed] [Google Scholar]

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