Properties of cod metallothionein,its presence in different tissues and effects of Cd and Zn treatment |
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Authors: | K Hylland C Haux C Hogstrand K Sletten R A Andersen |
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Institution: | 1. Section of Marine Zoology and Marine Chemistry, Department of Biology, University of Oslo, P.O. Box 1064, N-0316, Oslo, Norway 3. Department of Biochemistry, University of Oslo, P.O. Box 1041, N-0316, Oslo, Norway 2. Department of Zoophysiology, University of G?teborg, Medicinaregatan 18, S-41 390, G?teborg, Sweden
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Abstract: | One isoform of the low-molecular-weight metal-binding protein metallothionein (MT) has been isolated from the liver of Atlantic
cod by size-exclusion and ion-exchange chromatography. Cod MT contained 33% cysteine, no aromatic amino acids or arginine.
As is the case for other piscine MTs, the N-terminus of cod MT lacked the asparagine in position 4 which is present in mammalian
MTs. In addition, cod MT differed from all other vertebrate MTs described in that the N-terminal methionine was not acetylated.
Antibodies were raised in rabbits against hepatic MT from cod by repeated injections of native protein mixed with adjuvant.
Anti-cod MT antisera cross reacted with similarly-sized proteins in liver, brain, anterior kidney, posterior kidney, spleen,
intestine, gills and ovaries. The putative MT in cod brain migrated differently to that of the other tissues in native gel
electrophoresis. Intraperitoneally injected Cd (1 mg/kg) was nearly entirely associated with the MT-peak in hepatic and renal
cytosols, whereas a single injection of Zn (10 mg/kg) resulted in increases in all cytosolic Zn pools of the liver and no
apparent change in cytosolic Zn, Cu, Ni or Cd in kidney. |
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Keywords: | metallothionein Gadus morhua liver anterior kidney brain PAGE immunoblotting N-terminal sequence amino acid composition |
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