02043nam a2200229Ia 4500003001000000005001700010040000900027245008900036490006000125520125000185650002001435650002301455650001701478650001801495650002701513700001901540700001601559700002401575700001701599856015601616008004101772MX-MdCICY20260521091343.0  cCICY10aTwo uncommon phospholipase D isoenzymes from poppy seedlings (Papaver somniferum L.)0 vBiochimica et Biophysica Acta, 1631(2), p.153-159, 20033 aPhospholipase D (PLD)has been detected in seedlings of Papaver somniferum L. cv. Lazu´ r (Papaveraceae). Purification of the enzyme revealed the existence of two forms of PLD (named as PLD-A and PLD-B). The two enzymes strongly differ in their catalytic properties. The pH optima were found at pH 8.0 for PLD-A and at pH 5.5 for PLD-B. While both enzymes show hydrolytic activity toward phosphatidylcholine (PC)and phosphatidyl-p-nitrophenol (PpNP), PLD-B only was able to catalyze the exchange of choline in PC by glycerol. Both enzymes were activated by Ca2 + ions with an optimum concentration of 10 mM. In contrast to PLDs from other plants, LD-B was still more activated by Zn2 + ions with an optimum concentration of 5 mM. The apparent molecular masses of PLD-A and PLD-B, derived from sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE), were estimated to be 116.4 and 114.1 kDa. N-terminal protein sequencing indicated N-terminal blockage in both cases. The isoelectric points were found to be 8.7 for PLD-A and 6.7 for PLD-B. Both enzymes were shown to be N-linked glycoproteins. This paper is the first report on PLD in poppy and indicates some important differences of the two enzyme forms to other PLDs known so far.14aPHOSPHOLIPASE D14aPAPAVER SOMNIFERUM14aPURIFICATION14aZN-ACTIVATION14aTRANSPHOSPHATIDYLATION12aOblozinsky, M.12aSchoeps, R.12aUlbrich-Hofmann, R.12aBezakova, L.40uhttps://drive.google.com/file/d/1Xmvhn1XCXbNqiSWKDEylY0DIrqQh8SGu/view?usp=drivesdkzPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx250602s9999    xx |||||s2   |||| ||und|d