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  • Title: Purification and characterization of acetyl esterase from bull testes.
    Author: Arav R, Rimon S.
    Journal: Biochim Biophys Acta; 1987 Dec 18; 916(3):313-20. PubMed ID: 3689793.
    Abstract:
    Acetyl esterase (acetic-ester acetylhydrolase, EC 3.1.1.6) from bull testes was purified 325-fold by ammonium sulphate precipitation, chromatography on DEAE-cellulose, hydroxyapatite and finally, gel filtration on a Sephadex G-200 column. The purified enzyme appeared as a single protein band on native polyacrylamide gel electrophoresis and in isoelectric focusing (pI 5.25). In both methods, the activity coincided with the protein band. A single protein band corresponding to Mr 70,000 was obtained by SDS-polyacrylamide gel electrophoresis. The reported amino-acid composition indicates that the enzyme contains three half-cystine residues, of which only one could be detected, by titration, as a free -SH group. No free amino terminal was detected by dansylation.
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