Purification and characterization of acetyl esterase from bull testes.
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.
Arav
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Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel.
Rimon
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D000115:Acetylesterase / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D007526:Isoelectric Point; D008297:Male; D008970:Molecular Weight; D013737:Testis / Q000201:enzymology*
D000596:Amino Acids; D000115:Acetylesterase