Hemoglobin-like proteins found in the single-celled organisms.
| Project/Area Number |
06640874
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
動物生理・代謝
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| Research Institution | TOHOKU UNIVERSITY |
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Principal Investigator |
MATSUOKA Ariki Tohoku Univ.Graduate School of Sci. Research Assistant, 大学院理学研究科, 助手 (30222293)
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| Co-Investigator(Kenkyū-buntansha) |
TAJIMA Gen-ichi Tohoku Univ. Graduate School of Sci. Research Assistant, 大学院理学研究科, 助手 (00197360)
SHIKAMA Keiji Tohoku Univ.Graduate School of Sci. Professor, 大学院理学研究科, 教授 (40004337)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1995: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1994: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | protozoa / yeast / hemoglobin / autoxidation / distal histidine / myoglobin / 遠位ヒステジン |
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| Research Abstract |
(1) We have succeeded in isolating a hemoglobin-like protein from a ciliated protozoa (Tetrahymena pyriformis) by using gel filtration on Sephadex G-50 followed by CM-celluloce chromatography. The Soret absorption and magnetic-circular-dichroic spectra for its ferric met form were very similar to those of mammalian myoglobins, indicating that its axial water molecule is stabilized probably by a distal histidine residue.
(2) A hemoglobin-like protein was directly isolated from yeast (Candida norvegensis) and its CD spectrum was measured in 10 mM phosphate buffer, pH7.0. The resultant mean residue molar ellipticity at 222 nm was found to be-13700 deg cm^2 dmol^<-1>, this value being extremely unusual as compared with [rheta]^<MRW>_=-25400 deg cm^2 dmol^<-1> for sperm whale myoglobin used as a reference. On the basis of several lines of evidence, we propose an unique structure of yeast hemoglobin.
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Report
(3 results)
Research Products
(14 results)
