Purification of Turkey Pancreatic Phospholipase A_2(Biochemistry & Molecular Biology)
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概要
- 論文の詳細を見る
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 14kDa. The optimal activity was measured at pH 8 and 37℃ using egg yolk emulsion as substrate. Our results show that the enzyme (TPP) was not stable for 1 h at 60℃, and that bile salt and Ca^<2+> 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.
- 社団法人日本農芸化学会の論文
- 2003-10-23
著者
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Salah Riadh
Laboratoire De Biochimie Et De Genie Enzymatique Des Upases Ecole Nationale Des Ingenieurs De Sfax
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Salah Riadh
Laboratory Of Biochemistry
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Mejdoub Hafedh
Laboratoire de Biochimie et de Genie enzymatique des Upases, Ecole Nationale des Ingenieurs de Sfax
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Mejdoub Hafedh
Laboratoire De Biochimie Et De Genie Enzymatique Des Lipases
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Mejdoub Hafedh
Laboratory Of Biochemistry Faculty Of Sciences Of Sfax
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ZOUARI Nacim
Laboratory of Biochemistry
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REINBOLT Joseph
IBMC
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