Identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin
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 det...
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fthokunivhus:oai:eprints.lib.hokudai.ac.jp:2115/39846 2023-05-15T18:32:52+02:00 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 http://hdl.handle.net/2115/39846 https://doi.org/10.1007/s12562-009-0165-2 eng eng Springer Japan http://hdl.handle.net/2115/39846 Fisheries Science, 75(6): 1445-1452 http://dx.doi.org/10.1007/s12562-009-0165-2 The original publication is available at www.springerlink.com Amine incorporation Carp Crosslinking Myosin heavy chain Subfragment 2 Transglutaminases Walleye pollack 663 article (author version) fthokunivhus https://doi.org/10.1007/s12562-009-0165-2 2022-11-18T01:01:53Z 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. Article in Journal/Newspaper Theragra chalcogramma Hokkaido University Collection of Scholarly and Academic Papers (HUSCAP) Fisheries Science 75 6 1445 1452 |
institution |
Open Polar |
collection |
Hokkaido University Collection of Scholarly and Academic Papers (HUSCAP) |
op_collection_id |
fthokunivhus |
language |
English |
topic |
Amine incorporation Carp Crosslinking Myosin heavy chain Subfragment 2 Transglutaminases Walleye pollack 663 |
spellingShingle |
Amine incorporation Carp Crosslinking Myosin heavy chain Subfragment 2 Transglutaminases Walleye pollack 663 Nozawa, Hisanori Ezou, Mai Identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin |
topic_facet |
Amine incorporation Carp Crosslinking Myosin heavy chain Subfragment 2 Transglutaminases Walleye pollack 663 |
description |
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. |
format |
Article in Journal/Newspaper |
author |
Nozawa, Hisanori Ezou, Mai |
author_facet |
Nozawa, Hisanori Ezou, Mai |
author_sort |
Nozawa, Hisanori |
title |
Identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin |
title_short |
Identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin |
title_full |
Identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin |
title_fullStr |
Identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin |
title_full_unstemmed |
Identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin |
title_sort |
identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin |
publisher |
Springer Japan |
url |
http://hdl.handle.net/2115/39846 https://doi.org/10.1007/s12562-009-0165-2 |
genre |
Theragra chalcogramma |
genre_facet |
Theragra chalcogramma |
op_relation |
http://hdl.handle.net/2115/39846 Fisheries Science, 75(6): 1445-1452 http://dx.doi.org/10.1007/s12562-009-0165-2 |
op_rights |
The original publication is available at www.springerlink.com |
op_doi |
https://doi.org/10.1007/s12562-009-0165-2 |
container_title |
Fisheries Science |
container_volume |
75 |
container_issue |
6 |
container_start_page |
1445 |
op_container_end_page |
1452 |
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1766217062275874816 |