| Project/Area Number |
62540551
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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 |
動物発生・生理学
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| Research Institution | Kouch University |
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Principal Investigator |
FURUKOHRI Takahiro Kouch Univ., Fac. of Sci., Professor, 理学部, 教授 (30036553)
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| Co-Investigator(Kenkyū-buntansha) |
SUZUKI Tomohiko Kouch Univ., Fac. of Sci., Assistant, 理学部, 助手 (60145109)
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| Project Period (FY) |
1987 – 1989
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| Project Status |
Completed (Fiscal Year 1989)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1989: ¥300,000 (Direct Cost: ¥300,000)
Fiscal Year 1988: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1987: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | Myoglobin / Amino acid sequence / Mollusc / Didomain structure / Sulculus / Bursatella / ドメイン |
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| Research Abstract |
Myoglobins from the gastropodic molluscs, Sulculus diversicolor aquatilis and Bursatella leachii were investigated.
1. An usual myoglobin was isolated from the buccal mass of the ear-shell Sulculus diversicolor aquatilis. The myoglobin consists of a 39kDa polypeptide chain which is about double the size of the usual myoglobin subunit, contains one heme per molecule, and has an unusual spectral property in the oxy-form. On the basis of these properties and partial amino acid sequencing, we propose that Sulculus myoglobin has a didomain structure, and that one of the two domains does not function as an oxygen-binding domain. So far, a myoglobin of this type has not been described in molluscs.
2. The complete amino acid sequence of myoglobin from the triturative stomach of gastropodic mollusc Bursatella Leachii has been determined. It is composed of 146 amino acid residues, is acetylated at the N-terminus, and contains a single histidine residue position 95 which corresponds to the heme-binding proximal histidine. The E7 distal histidine, which is conserved widely in myoglobins and hemoglobins, is replaced by valine in Bursatella myoglobin. The amino acid sequence of Bursatella myoglobin shows strongly homology (73 - 84%) with those of Aplysia and Dolabella myoglobins.
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