Identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin

• Nozawa, Hisanori

• Ezou, Mai

抄録

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.

収録刊行物

• Fisheries Science

  Fisheries Science 75 (6), 1445-1452, 2009-11

  Springer Japan

キーワード

• Amine incorporation
• Carp
• Crosslinking
• Myosin heavy chain
• Subfragment 2
• Transglutaminases
• Walleye pollack

詳細情報

• CRID: 1050564288955625344
• NII論文ID: 10025444479
• NII書誌ID: AA10993718
• HANDLE: 2115/39846
• ISSN: 09199268
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles