Purification and biochemical characterization of a lysosomal copper-rich thionein-like protein involved in metal detoxification in the digestive gland of mussels

1. The lysosomal insoluble Cu-rich protein present in the digestive gland of metal-exposed mussels ( Mytilus galloprovincialis Lam.) was extracted and biochemically characterized. 2. The solubilized Cu-protein shows Chromatographic and electrophoretic properties similar to those of mussel metallothi...

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Published inComparative biochemistry and physiology. C, Comparative pharmacology Vol. 93; no. 2; pp. 389 - 395
Main Authors Viarengo, A., Pertica, M., Canesi, L., Mazzucotelli, A., Orunesu, M., Bouquegneau, J.M.
Format Journal Article
LanguageEnglish
Published Oxford Elsevier B.V 1989
New York, NY Pergamon Press
Subjects
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Invertebrates
Mollusca
Physiology. Development
Cell organelle
Purification
Digestive system
Lysosome
Detoxication
Metal
Mytilus galloprovincialis
Chromatography
Marine environment
Proteins
Bivalvia
Digestive gland
Invertebrata
Mollusca
Copper
Metallothionein
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Summary:1. The lysosomal insoluble Cu-rich protein present in the digestive gland of metal-exposed mussels ( Mytilus galloprovincialis Lam.) was extracted and biochemically characterized. 2. The solubilized Cu-protein shows Chromatographic and electrophoretic properties similar to those of mussel metallothioneins. 3. The UV spectrum of the purified lysosomal Cu-protein is typlcal of Cu-thioneins; it consistently shows an amino acid composition similar to that of previously characterized cytosolic metallothioneins. It differs, however, in that it has a low glycine content as well as a high level of aspartic and glutamic acid. 4. The possible role of lysosomes in metallothionein metabolism is discussed.
ISSN:0306-4492
DOI:10.1016/0742-8413(89)90252-1