The quaternary structure of the lobster carapace carotenoprotein,crustacyanin: Studies using cross-linking agents |
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| Institution: | 1. Department of Biochemistry, Royal Holloway and Bedford New College, Egham Hill, Egham, Surrey TW20 0EX, UK (Tel: 0784 434455);2. Department of Biophysics and Biochemistry, Leeds University, Leeds LS2 9JT, UK;1. Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Phyathai Road, Bangkok 10330, Thailand;2. National Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), 113 Paholyothin Road, Klong1, Klong Luang, Pathumthani 12120, Thailand;1. Graduate School of Marine Science and Technology, Tokyo University of Marine Science and Technology, Tokyo, Japan;2. Institute of Aquaculture, College of Fisheries and Ocean Sciences, University of the Philippines Visayas, Miagao, Iloilo, Philippines;3. Department of Marine Science, College of Science and Mathematics, Mindanao State University-Iligan Institute of Technology, Iligan City, Philippines;1. Department of Chemistry, Faculty of Science, Srinakharinwirot University, Bangkok, 10110, Thailand;2. Department of Biology, Faculty of Science, King Mongkut''s Institute of Technology Ladkrabang, Bangkok, 10520, Thailand;3. Center for Vaccine Development, Institute of Molecular Biosciences, Mahidol University, 25/25 Phuttamonthon 4 Road, Salaya, Nakhon Pathom, 73170, Thailand;4. National Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), Pathum Thani, 110120, Thailand;5. Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand |
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| Abstract: | - 1.1. Three bis(imidoesters) of different span (ca 9–11 Å) have been used to form intermolecular cross-links between the apoproteins of the lobster carapace carotenoprotein, α-crustacyanin.
- 2.2. Dimethylpimelimidate(DMP) is the most effective of the three reagents in cross-linking the oligomeric α-crustacyanin, giving predominantly dimers between apoproteins from each of the two apoprotein classes. The native dimers, β-crustacyanins, are effectively cross-linked with this reagent.
- 3.3. The stability of DMP cross-linked α-crustacyanin and of the native carotenoprotein to urea treatment and to heating have been compared.
- 4.4. Reagents of longer (sulpho-N-hydroxy-succinimide ester; 18 Å) or shorter (1,5-difluoro-2,4-dinitrobenzene; 5 Å) spans than the bis(imidoesters) are similarly able to form cross-linked dimers with the crustacyanins, but less effectively under the conditions of the reactions.
- 5.5. The results are discussed in relation to the previously presented putative structure of β-crustacyanin (Keen et al. 1990b. Eur. J. Biochem. (submitted); Zagalsky et al., 1990. Comp. Biochem. Physiol.97B, 1–18) and to an alternative subunit interface arrangement of the apoproteins for the dimer.
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