| Autor: |
Moll GN; C.B.L.E., State University of Utrecht, The Netherlands., Vial HJ, van der Wiele FC, Ancelin ML, Roelofsen B, Slotboom AJ, de Haas GH, van Deenen LL, Op den Kamp JA |
| Jazyk: |
angličtina |
| Zdroj: |
Biochimica et biophysica acta [Biochim Biophys Acta] 1990 May 09; Vol. 1024 (1), pp. 189-92. |
| DOI: |
10.1016/0005-2736(90)90224-c |
| Abstrakt: |
Pig pancreatic phospholipase A2 does not act on normal erythrocytes, but the membrane penetrating capacity is enhanced by the covalent attachment of one fatty acyl chain to Lys-116 of the enzyme. Taking advantage of the impaired packing of phospholipids in the membrane of Plasmodium infected erythrocytes it was demonstrated that a lauric acid derivative of phospholipase A2 is capable of exclusively attaching the infected erythrocytes in vitro, leaving the uninfected cells undisturbed. The chemically modified phospholipase A2 appeared to cause death of the parasite in cell cultures of infected erythrocytes. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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