The polymerization of protein through disulfide bonding during the heating of carp myosin
The polymer of protein through SS bonding on the top of 5% SDS-PAGE gel was found to be made up of only a myosin heavy chain from the analysis of two-step SDS-PAGE, and from the results it was a dimer, trimer, tetramer, and above-decamer with 1.8% SDS-PAGE gel. The polymerization was suppressed in t...
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| Veröffentlicht in: | NIPPON SUISAN GAKKAISHI 1995/01/25, Vol.61(1), pp.75-80 |
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| container_title | NIPPON SUISAN GAKKAISHI |
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| creator | Kishi, A. (Kochi Univ., Nankoku (Japan). Faculty of Agriculture) Itoh, Y Obatake, A |
| description | The polymer of protein through SS bonding on the top of 5% SDS-PAGE gel was found to be made up of only a myosin heavy chain from the analysis of two-step SDS-PAGE, and from the results it was a dimer, trimer, tetramer, and above-decamer with 1.8% SDS-PAGE gel. The polymerization was suppressed in the presence of N-ethylmaleimide, dithiothreitol, or EDTA. The polymerization of myosin light chains as well as myosin heavy chain was promoted in the presence of transition ion (Cu+, Cu2+), while Ca2+ and Mg2+ did not affect the polymerization. From the above results, it was made clear that the polymerization of protein through SS bonding during the heating of myosin is the reaction that the SH groups of myosin heavy chain are oxidized in the presence of catalysts such as copper ion, and contribute to the smooth and swift formation of the polymer larger than decamer. |
| doi_str_mv | 10.2331/suisan.61.75 |
| format | Article |
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(Kochi Univ., Nankoku (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Itoh, Y</creatorcontrib><creatorcontrib>Obatake, A</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Environment Abstracts</collection><collection>Oceanic Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Environment Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>NIPPON SUISAN GAKKAISHI</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kishi, A. (Kochi Univ., Nankoku (Japan). 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The polymerization of myosin light chains as well as myosin heavy chain was promoted in the presence of transition ion (Cu+, Cu2+), while Ca2+ and Mg2+ did not affect the polymerization. From the above results, it was made clear that the polymerization of protein through SS bonding during the heating of myosin is the reaction that the SH groups of myosin heavy chain are oxidized in the presence of catalysts such as copper ion, and contribute to the smooth and swift formation of the polymer larger than decamer.</abstract><cop>Tokyo</cop><pub>The Japanese Society of Fisheries Science</pub><doi>10.2331/suisan.61.75</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng ; jpn |
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| source | J-STAGE Free; EZB-FREE-00999 freely available EZB journals; AgriKnowledge（アグリナレッジ）AGROLib |
| subjects | CARP CARPA CARPE CATALIZADOR CATALYSEUR CATALYSTS CHEMICAL REACTIONS COBRE COMPOSE ORGANOSOUFRE COMPUESTO ORGANICO DEL AZUFRE COPPER CUIVRE Cyprinus carpio GLOBULINAS GLOBULINE GLOBULINS HEAT TREATMENT ION IONES IONS ORGANOSULPHUR COMPOUNDS OXIDACION OXIDATION OXYDATION POLIMERIZACION POLYMERISATION POLYMERIZATION REACCIONES QUIMICAS REACTION CHIMIQUE TRAITEMENT THERMIQUE TRATAMIENTO TERMICO |
| title | The polymerization of protein through disulfide bonding during the heating of carp myosin |
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