Studies on resilin biosynthesis |
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| Authors: | G C Coles |
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| Affiliation: | 1. KTH Royal Institute of Technology, School of Chemical Sciences and Engineering, Department of Chemistry, Surface and Corrosion Science, Drottning Kristinas Väg 51, SE-10044 Stockholm, Sweden;2. Medicinal Biochemistry and Microbiology, Institute of Biomedicine, University of Gothenburg, Medicinaregatan 9A, SE-40530 Gothenburg, Sweden;3. SP Technical Research Institute of Sweden, SP Chemistry, Materials and Surfaces, Box 5607, SE-114 86 Stockholm, Sweden;1. Department of Anatomy and Pathology, Joan C. Edwards School of Medicine, Marshall University, Huntington, WV 25704, USA;2. Department of Biological Cybernetics, University of Bielefeld, 33501 Bielefeld, Germany;3. Department of Animal Physiology, Institute of Zoology, Biocenter Cologne, University of Cologne, 50923 Cologne, Germany;1. Department of Biological Sciences, Tokyo Metropolitan University, Japan;2. Department of Liberal Arts and Human Development, Kanagawa University of Human Services, Japan;1. Senckenberg German Entomological Institute, Eberswalder Str. 90, 15374, Müncheberg, Germany;2. Evolutionary Biology of Invertebrates, Institute of Evolution and Ecology, Eberhard Karls University of Tübingen, Auf der Morgenstelle 28E, 72076, Tübingen, Germany;1. College of Chemistry, Chemical Engineering and Material Science, Soochow University, 199 Ren-ai Road, Suzhou, 215123, Jiangsu Province, People''s Republic of China;2. Department of Chemical Engineering, University of Waterloo, Waterloo, Ontario, N2L 3G1, Canada |
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| Abstract: | The cells that deposit resilin in Schistocerca gregaria have been studied to test the hypothesis that this protein is formed by the cross-linking of proresilin by a peroxidase enzyme. A peroxidase, resembling that from horse-radish, is present in these cells, and also in the gut, flight muscle, and cuticle with attached epidermal cells. There are proteins in the cells that deposit resilin that can be cross-linked by the peroxidase enzyme to form di- and trityrosine residues. However, it cannot be concluded that the natural function of the peroxidase enzyme is to cross-link proresilin and similar cuticular proteins because it has not been possible to demonstrate its presence in the cuticle or at the surface of the epidermal cells. Some observations on chitin synthesis by these cells are reported. |
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