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. 1967 Apr;103(1):29–35. doi: 10.1042/bj1030029

Immunochemistry of sperm-whale myoglobins prepared with various modified porphyrins and metalloporphyrins

M Z Atassi 1
PMCID: PMC1270364  PMID: 6068005

Abstract

1. The preparation and characterization of manganese, iron, cobalt, nickel, copper and zinc metalloporphyrins is described. Ferrihaem was also esterified with pyrid-4-ylpropanol and the derivative characterized as the diester. 2. Complexes of these various porphyrins, as well as protoporphyrin IX, with apomyoglobin were formed and the resulting artificial myoglobins characterized. 3. Very little complex-formation was obtained with nickel, cobalt and manganese metalloporphyrins and apomyoglobin. 4. Myoglobin prepared with copper metalloporphyrin was immunochemically identical with native ferrimyoglobin. All the other artificial myoglobins were less reactive to varying degrees. 5. The changes in antigenic reactivities were attributed to conformational reorganization caused by the different co-ordination tendencies of the various metals or by the modification of the side chains of the haem.

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Selected References

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

  1. ATASSI M. Z. PROPERTIES OF COMPONENTS OF MYOGLOBIN OF THE SPERM WHALE. Nature. 1964 May 2;202:496–498. doi: 10.1038/202496a0. [DOI] [PubMed] [Google Scholar]
  2. Atassi M. Z., Brown R. K., McEwan M. Immunochemical studies of hemoglobin and the role of the sulfhydryl groups. Immunochemistry. 1965 Dec;2(4):379–389. doi: 10.1016/0019-2791(65)90037-6. [DOI] [PubMed] [Google Scholar]
  3. Atassi M. Z. Periodate oxidation of sperm-whale myoglobin and the role of the methionine residues in the antigen-antibody reaction. Biochem J. 1967 Feb;102(2):478–487. doi: 10.1042/bj1020478. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Crumpton M. J., Wilkinson J. M. The immunological activity of some of the chymotryptic peptides of sperm-whale myoglobin. Biochem J. 1965 Mar;94(3):545–556. doi: 10.1042/bj0940545. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hill R., Holden H. F. The Preparation and some Properties of the Globin of Oxyhaemoglobin. Biochem J. 1926;20(6):1326–1339. doi: 10.1042/bj0201326. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. KENDREW J. C., WATSON H. C., STRANDBERG B. E., DICKERSON R. E., PHILLIPS D. C., SHORE V. C. The amino-acid sequence x-ray methods, and its correlation with chemical data. Nature. 1961 May 20;190:666–670. doi: 10.1038/190666a0. [DOI] [PubMed] [Google Scholar]
  7. MCCONNEL R. J., OVERELL B. G., PETROW V., STURGEON B. The chemistry of anti-pernicious anaemia factors. XI. The preparation and properties of some cobalt porphyrins. J Pharm Pharmacol. 1953 Mar;5(3):179–195. doi: 10.1111/j.2042-7158.1953.tb13974.x. [DOI] [PubMed] [Google Scholar]
  8. Markham R. A steam distillation apparatus suitable for micro-Kjeldahl analysis. Biochem J. 1942 Dec;36(10-12):790–791. doi: 10.1042/bj0360790. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. POULIK M. D. Starch gel electrophoresis in a discontinous system of buffers. Nature. 1957 Dec 28;180(4600):1477–1479. doi: 10.1038/1801477a0. [DOI] [PubMed] [Google Scholar]
  10. REICHLIN M., HAY M., LEVINE L. IMMUNOCHEMICAL STUDIES OF HEMOGLOBIN AND MYOGLOBIN AND THEIR GLOBIN MOIETIES. Biochemistry. 1963 Sep-Oct;2:971–979. doi: 10.1021/bi00905a013. [DOI] [PubMed] [Google Scholar]
  11. ROSSI-FANELLI A., ANTONINI E., CAPUTO A. Light scattering and sedimentation of native human adult and fetal globin. J Biol Chem. 1959 Nov;234:2906–2910. [PubMed] [Google Scholar]
  12. TEALE F. W. Haem-globin equilibrium studies by fluorimetry. Biochim Biophys Acta. 1959 Sep;35:289–291. doi: 10.1016/0006-3002(59)90376-2. [DOI] [PubMed] [Google Scholar]

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