1995 Fiscal Year Final Research Report Summary
Study on the linker chains of annelid giant hemoglobins
| Project/Area Number |
06640882
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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 | University of Tokushima |
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Principal Investigator |
GOTOH Toshio Univ.of Tokushima, Dep.of Life Sciences Professor, 総合科学部, 教授 (90035692)
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| Project Period (FY) |
1994 – 1995
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| Keywords | Hemoglobin / Lectin / Annelid / Carbohydrate gluing / Supramolecule / ESI-MS / LDl receptor |
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| Research Abstract |
The giant hemoglobins (Hb) of annelids are natural supramolecules consisting of about 200 polypeptide chains. We have reported a carbohydrate-dependent supramolecular arichitecture in the extracellular giant Hb from the marine worm Perinereis aibuhitensis ; we call this architectural mechanism carbohydrate gluing. This study is an extension of our accidental discovery of deterioration in the form of the Hb caused by a high concentration of glucose. We found that two types of linker chains "L1" and "L2" and globins "a" and "A" contained carbohydrates. Several monosaccharides tested reversibly dissociated the intact form of the Hb. We suggest that this carbohydrate gluing may be mediated through lectin-like carbohydarate-binding by the linker chains.
Electrospray ionization mass spectrometry (ESI-MS) of the extracellular Hb from the marine polychaete Tylorrhynchus heterochaetus provided a complete description of the polypeptide chain composition. The globin subunits consists of a monomer subunit (15575.4 Da) and a disulfide-bonded trimer subunit, 50068.4 Da. Linker subunits L1 and L2 with molecular masses of 23233.8 and 24835.4 Da, respectively, were found togather with a disulfide-bonded dimer of L2 (52609.4 Da).
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