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. 1975 Sep;12(3):297–298. doi: 10.1136/jmg.12.3.297

A new case of haemoglobin Bucuresti in a Cuban family: further functional studies.

B Colombe, M P Benitez, L Bernini, J Elien, H Wajeman, D Labie
PMCID: PMC1013293  PMID: 1177282

Abstract

A new case of haemoglobin Bucuresti beta 42 (CD1) Phe yields Leu is described in a Cuban family. The functional studies confirm the results already described--a low oxygen affinity and a decreased haem-haem interaction. In addition to this, the reactivity for 2, 3 diphosphoglycerate (2, 3 DPG) was shown to be normal. The instability is mostly due to a fast rate of haemichromes formation.

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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. BENESCH R., MACDUFF G., BENESCH R. E. DETERMINATION OF OXYGEN EQUILIBRIA WITH A VERSATILE NEW TONOMETER. Anal Biochem. 1965 Apr;11:81–87. doi: 10.1016/0003-2697(65)90045-x. [DOI] [PubMed] [Google Scholar]
  3. Bellingham A. J., Huehns E. R. Compensation in haemolytic anaemias caused by abnormal haemoglobins. Nature. 1968 Jun 8;218(5145):924–926. doi: 10.1038/218924a0. [DOI] [PubMed] [Google Scholar]
  4. Beutler E., Meul A., Wood L. A. Depletion and regeneration of 2,3-diphosphoglyceric acid in stored red blood cells. Transfusion. 1969 May-Jun;9(3):109–115. doi: 10.1111/j.1537-2995.1969.tb05527.x. [DOI] [PubMed] [Google Scholar]
  5. Bratu V., Lorkin P. A., Lehmann H., Predescu C. Haemoglobin Buccureşti 42(CD1) Phe-Leu, a cause of unstable haemoglobin haemolytic anaemia. Biochim Biophys Acta. 1971 Oct;251(1):1–6. doi: 10.1016/0005-2795(71)90051-1. [DOI] [PubMed] [Google Scholar]
  6. Brimhall B., Jones R. T., Baur E. W., Motulsky A. G. Structural characterization of hemoglobin Tacoma. Biochemistry. 1969 May;8(5):2125–2129. doi: 10.1021/bi00833a051. [DOI] [PubMed] [Google Scholar]
  7. Dacie J. V., Shinton N. K., Gaffney P. J., Jr, Lehmann H. Haemoglobin Hammersmith (beta-42 (CDI) Phe replaced by ser). Nature. 1967 Nov 18;216(5116):663–665. doi: 10.1038/216663a0. [DOI] [PubMed] [Google Scholar]
  8. Hartley B. S. Strategy and tactics in protein chemistry. Biochem J. 1970 Oct;119(5):805–822. doi: 10.1042/bj1190805f. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. JONES R. T. STRUCTURAL STUDIES OF AMINOETHYLATED HEMOGLOBINS BY AUTOMATIC PEPTIDE CHROMATOGRAPHY. Cold Spring Harb Symp Quant Biol. 1964;29:297–308. doi: 10.1101/sqb.1964.029.01.032. [DOI] [PubMed] [Google Scholar]
  10. Keeling M. M., Ogden L. L., Wrightstone R. N., Wilson J. B., Reynolds C. A., Kitchens J. L., Huisman T. H. Hemoglobin Louisville (beta-42 (CD1) phe-leu): an unstable variant causing mild hemolytic anemia. J Clin Invest. 1971 Nov;50(11):2395–2402. doi: 10.1172/JCI106738. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Rosemeyer M. A., Huehns E. R. On the mechanism of the dissociation of haemoglobin. J Mol Biol. 1967 Apr 28;25(2):253–273. doi: 10.1016/0022-2836(67)90141-6. [DOI] [PubMed] [Google Scholar]
  12. Wajcman H., Leroux A., Labie D. Functional properties of hemoglobin Hammersmith. Biochimie. 1973;55(2):119–126. doi: 10.1016/s0300-9084(73)80383-9. [DOI] [PubMed] [Google Scholar]

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