Carboxylic ester hydrolases in mitochondria from rat skeletal muscle
Research output: Contribution to journal › Journal article › Research › peer-review
A mitochondrial pellet, prepared from rat skeletal muscle, contained a number of carboxylic ester hydrolase isoenzymes. The esterases which split alpha-naphthyl acetate were organophosphate sensitive, whereas two out of three indoxyl acetate hydrolysing enzymes were resistant to both organophosphate and organomercury. The activity of the indoxyl acetate esterases was enhanced by the non-ionic detergents Tween-40 and Lubrol. After freezing, thawing and high speed centrifugation most of the alpha-naphthyl acetate splitting enzymes were found in the supernatant, indicating that the enzymes are loosely bound to mitochondrial membranes.
Original language | English |
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Journal | Journal of Molecular Histology (Print Edition) |
Volume | 22 |
Issue number | 2 |
Pages (from-to) | 95-101 |
Number of pages | 6 |
ISSN | 1567-2379 |
Publication status | Published - 1990 |
Bibliographical note
Keywords: Animals; Carboxylic Ester Hydrolases; Centrifugation; Detergents; Edetic Acid; Enzyme Inhibitors; Freezing; Isoenzymes; Male; Mersalyl; Mitochondria, Muscle; Muscles; Rats; Rats, Inbred Strains; Tritolyl Phosphates
ID: 10141011