Responsibility of Myosin S-1 and Rod for the Polymerization of Myosin Heavy Chain through Disulfide Bonding upon Heating of Actomyosin

• Runglerdkriangkrai Jiraporn

  Department of Aquaculture, Faculty of Agriculture, Kochi University

• Itoh Yoshiaki

  Department of Aquaculture, Faculty of Agriculture, Kochi University

• Kishi Akira

  Department of Aquaculture, Faculty of Agriculture, Kochi University

• Obatake Atsushi

  Department of Aquaculture, Faculty of Agriculture, Kochi University

Abstract

To elucidate the role of S-1 and rod in the polymerization of myosin heavy chain through SS bonding upon heating of actomyosin, each myofibril of carp (with 100μg/ml leupeptin), flying fish and rabbit was digested by ∝-chymotrypsin to S-1 and rod followed by heating for 1h at temperatures ranging from 10 to 80°C with added Cu²⁺ 12μM for carp and 100μM for other samples to enhance the oxidation of SH groups. SDS-PAGE and the measurement of SH content and surface hydrophobicity were performed. Behaviors of S-1 and rod from 3 species in common were as follows.<br> With the rising of temperature above 30°C, polymer at the top of 3% gel through SS bonding gradually increased with the concomitant decrease in S-1 and actin with Cu²⁺, while less polymer was found without Cu²⁺. This polymer was confirmed to be composed of S-1 and less amount of actin by two-step SDS-PAGE. Rod dimer through SS bonding was found almost at any heating temperatures except at 50°C where the degradation of rod occurred strongly.<br> Surface hydrophobicity increased clearly from 30°C, followed by gradual increase above 50°C. This behavior coincided very well with the increasing behavior of RSH upon heating without Cu²⁺. Oxidation of TSH was promoted with added Cu²⁺ slightly up to 30°C and greatly above 30°C, while RSH did so only a little below 30°C, and then greatly above 40°C in flying fish and 50°C in rabbit.<br> It was, therefore, concluded that the polymer formation of HC upon heating of actomyosin was mainly due to the oxidation of SH groups in S-1, while the dimer formation of HC was due to the oxidation of SH groups in rod.

Journal

• Fisheries science

  Fisheries science 65 (2), 310-314, 1999

  The Japanese Society of Fisheries Science

Keywords

• myosin heavy chain
• S-1
• rod
• disulfide bond
• heat denaturation
• polymerization
• sulfhydryl groups
• surface hydrophobicity

Details

• CRID: 1390282679406443648
• NII Article ID: 130003903358
• NII Article ID: 10004878579
• NII Book ID: AA10993718
• DOI: 10.2331/fishsci.65.310
• NDL BIB ID: 4706665
• ISSN: 09199268
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I4706665
• Web Site: https://www.jstage.jst.go.jp/article/fishsci1994/65/2/65_2_310/_pdf
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed