1987 Fiscal Year Final Research Report Summary
The allosteric effect in hemoglobin.
| Project/Area Number |
60304099
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| Research Category |
Grant-in-Aid for Co-operative Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
生物物性学
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| Research Institution | Faculty of Engineering Science Osaka University |
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Principal Investigator |
MORIMOT H. Associate professor, Faculty of Engineering Scinece, Osaka Univ., 基礎工学部, 助教授 (20029474)
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| Co-Investigator(Kenkyū-buntansha) |
IMAI K. Associate professor, Osaka Univ. Medical School, 医学部, 助教授 (50028528)
KITAGAWA T. Professor, Institute for Molecular Science, Okazaki National Research Institute, 教授 (40029955)
GO N. Professor, Faculty of Science, Kyoto Univ., 理学部, 教授 (50011549)
小西 康子 北里大学, 医学部, 助手 (80129238)
KAJITA A. Professor, Dokkyo Univ. Shool of Medicine, 教授 (80049113)
KAWAMURA-KONISHI Y. Research Assistant, Kitasato Univ. School of Medicine
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| Project Period (FY) |
1985 – 1987
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| Keywords | Hemoglobin / Allosteric / Metalloporphyrin / Conformation / Bohr Effect / Two state model / Intermediate / 2状態モデル |
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| Research Abstract |
1) The conformational changes of various parts ot a deoxyhemoglobin molecule were investigated when its oxygen affinity was altered by use of abnormal hemoglobins and chemically modified ones. It was found that the conformational changes around heme and those of the globin moiety did not take place in concerted manner on the contrary to the expectation of the two state allosteric model. 2) Four metalloprotoporphyrins were found to medel the deoxyheme. Among them Ni-protoporphyrinIX has been studied most extensively. Judging from the oxygen equilibrium properties of Ni-Fe hybrid hemoglobins. Ni-protoporphyrinIX behaves just like "frozen" deoxyheme not only in unmodified hemoglobins but also in modified ones. 3) The model for the intermediate state of the oxygenation of hemoglobin prepared by use of Ni-protoporphyrin showed a conformational state, which could not be accomodated in the framework of the two state allosteric model. 4) The interaction between the electronic state of iron and the globin moiety was investigated by substituteing iron serries transition metal ions for iron. The conformational state of the hemoglobin having the metalloprotoporphyrin changed according to the position of the element in the periodical table. No complete explanation of the result has been given. 5) Data were obtained to suggest the importance of the 1 1 interaction. 6) 89 Histidine was shown to contribute about 25% of the alkaline Bohr effect. 7) It became possible to prepare a hemoglobin having any primary structure by gene manipulation of E. coli. 8) An equipment to measure a resonance Raman spectra excited by ultraviolet laser beams was constructed. 9) The dynamic three dimentional structure of myoglobin was analyed by the computer calculation of the conformational energy function.
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Research Products
(40 results)
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[Publications] Imai, K., Yoshikawa, S., Fushitani, K., Takizawa, H., Handa, T. & Kihara, H.: "Inference of allosteric unit in chlororuorin, erythrocruorin, and hemerythrin on the basis of the Monod-Wyman-Changeux model." Invertebrate Oxygen Carriers (B. Linzen, ed.) Springer-Verlag.367-374 (1986)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Wagner, G., Braun, W., Havel, T.F., Schaumann, T., Go, N. & Wuetrich, K.: "Protein Structures in Solution by Nuclear Magnetic Resonance and Distance Geometry: The Polypeptide Fold of the Basic Pancreatic Trypsin Inhibitor Determined Using Two Different Algorithms, Disgeo and Disman." J. Mol. Biol.196. 611-639 (1987)
Description
「研究成果報告書概要(欧文)」より
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