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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences >
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Identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin
| Title: | Identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin |
| Authors: | Nozawa, Hisanori Browse this author →KAKEN DB | | Ezou, Mai Browse this author |
| Keywords: | Amine incorporation | | Carp | | Crosslinking | | Myosin heavy chain | | Subfragment 2 | | Transglutaminases | | Walleye pollack |
| Issue Date: | Nov-2009 |
| Publisher: | Springer Japan |
| Journal Title: | Fisheries Science |
| Volume: | 75 |
| Issue: | 6 |
| Start Page: | 1445 |
| End Page: | 1452 |
| Publisher DOI: | 10.1007/s12562-009-0165-2 |
| Abstract: | In order to elucidate the molecular mechanism of transglutaminase-mediated myosin cross-linking, a fluorescent monodansylcadaverine (MDC) was incorporated into carp Cyprinus carpio myosin and the reactive Gln residues were analyzed by cyanogen bromide cleavage. The fluorescence was predominantly detected in a 10.5 kDa BrCN-fragment, which is assumed to be located in subfragment 2 of the myosin heavy chain. Furthermore, lysyl endopeptidase digestion of the 10.5 kDa fragment revealed that MDC was specifically incorporated into the 520th Gln residue of the subfragment 2 domain. When meat paste prepared from walleye pollack Theragra chalcogramma frozen surimi was incubated with MDC, the fluorescence was mostly observed in a 16 kDa BrCN-fragment and also slightly detected in other three bands. By the digestion of 16 kDa fragment with lysyl endopeptidase, it was elucidated that MDC was incorporated specifically into Gln-520 of myosin subfragment 2, as well as detected in carp. This domain around Gln-520 is likely to be a common critical region for dimer formation of myosin heavy chains for both fish species. In walleye pollack, other reactive Gln residues are presumed to be exist in the C-terminus of the light meromyosin. This slight difference may be significant in a capacity to form tetramers or even larger multimers. |
| Rights: | The original publication is available at www.springerlink.com |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/39846 |
| Appears in Collections: | 水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 埜澤 尚範
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