Glutathione S-transferase from the Icelandic scallop (Chlamys islandica): Isolation and partial characterization
| Autor: | Bjørnar Myrnes, Inge W. Nilsen |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
DNA
Complementary Physiology Health Toxicology and Mutagenesis Protein subunit Molecular Sequence Data Toxicology Biochemistry Gene product chemistry.chemical_compound stomatognathic system Chlamys islandica Complementary DNA Animals Amino Acid Sequence Glutathione Transferase chemistry.chemical_classification Base Sequence biology Cell Biology General Medicine Glutathione biology.organism_classification Gastrointestinal Tract Pectinidae Enzyme Glutathione S-transferase chemistry Scallop biology.protein Sequence Alignment |
| Zdroj: | Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology. 144:403-407 |
| ISSN: | 1532-0456 |
| DOI: | 10.1016/j.cbpc.2006.11.011 |
| Popis: | Glutathione S-transferase from the digestive gland of the cold-adapted marine bivalve Icelandic scallop was purified to apparent homogeneity by single GSTrap chromatography. The enzyme appeared to be a homodimer with subunit M(r) 22,000 having an optimum catalytic activity at pH 6.5-7. Enzymatic analysis of scallop GST using the substrates 1-chloro-2,4-dinitrobenzene (CDNB) and glutathione resulted in apparent values for K(m)(GST) and K(m)(CDNB) of 0.3 mM and 0.4 mM, respectively. The scallop GST lost activity faster than porcine GST when exposed to increased temperatures, but both enzymes needed 10 min incubation at 60 degrees C for complete inactivation. A partial coding sequence was identified in cDNA synthesised from digestive gland mRNA. Comparison to known sequences indicates that the gene product is a glutathione S-transferase, and the predicted Icelandic scallop GST protein scores 40% sequence identity and 60% sequence similarity to mu-class proteins. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect