02122nam a2200265Ia 4500 MX-MdCICY 20260521091343.0 CICY B-13250 Two uncommon phospholipase D isoenzymes from poppy seedlings (Papaver somniferum L.) Biochimica et Biophysica Acta, 1631(2), p.153-159, 2003 Phospholipase 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. PHOSPHOLIPASE D PAPAVER SOMNIFERUM PURIFICATION ZN-ACTIVATION TRANSPHOSPHATIDYLATION Oblozinsky, M. Schoeps, R. Ulbrich-Hofmann, R. Bezakova, L. https://drive.google.com/file/d/1Xmvhn1XCXbNqiSWKDEylY0DIrqQh8SGu/view?usp=drivesdk Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx Loc REF1 250602s9999 xx |||||s2 |||| ||und|d 23390 23390 0 0 Loc 0 0 F1 CICY CICY RE 2025-06-25 0 B-13250 2025-06-25 15:39:19 2025-06-25 REF1