1994 Fiscal Year Final Research Report Summary
Protozoan Myoglobin : Its structure, function and evolution
| Project/Area Number |
04454022
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
動物発生・生理学
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| Research Institution | Tohoku University |
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Principal Investigator |
SHIKAMA Keiji Biological institute, Tohoku University, Professor, 理学部, 教授 (40004337)
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| Co-Investigator(Kenkyū-buntansha) |
TAJIMA Genichi Biological institute, Tohoku University, Assistant, 理学部, 助手 (00197360)
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| Project Period (FY) |
1992 – 1994
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| Keywords | hemoglobin / Myoglobin / Protozoan / Primary Structure / CD / Autoisdebon / helix content / hewiohrome |
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| Research Abstract |
A hemoglobin-like protein is present in some of the single-celled organisms, but its structure is quite different from that of mammalian myoglobin or hemoglobin. For instance, a protozoan myoglobin isolated from Paramecium caudatum consists of 116 amino acid residues, so that this contracted form is nearly two thirds of sperm whale myoglobin. Yeast hemoglobin from Candida norvegensis, on the other hand, is composed of a single polypeptide chain of 387 amino acid residues, but of two distinct domains carrying different functions ; that is the N-terminal, heme-containing region and the C-terminal, FAD-containing reductase domain.
hemoglobin/myoglobin/protozoa (Paramecium caudatum) /yeast (Candida norvegensis) /amino acid sequence
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