Purification of turkey pancreatic phospholipase A2 |
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Authors: | Ben Salah Riadh Zouari Nacim Reinbolt Joseph Mejdoub Hafedh |
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Institution: | Laboratory of Biochemistry, ENIS Soukra Road, 3038 Sfax, Tunisia. |
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Abstract: | Turkey pancreatic phospholipase (TPP) has been purified from delipidated pancreases. The purification included ammonium sulfate fractionation, acidic (pH 5) treatment, followed by sequencial column chromatographies on DEAE-cellulose, Sephadex G-75, and reverse phase high pressure liquid chromatography. The purified enzyme was found to be a monomeric protein with molecular mass of 14 kDa. The optimal activity was measured at pH 8 and 37 degrees C using egg yolk emulsion as substrate. Our results show that the enzyme (TPP) was not stable for 1 h at 60 degrees C, and that bile salt and Ca2+ were required for the expression of the purified enzyme. The sequence of the N-terminal amino acids of the purified enzyme shows a very close similarity between TPP and all other known pancreatic phospholipases. |
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