Phospholipase A 2 from Trypanosoma congolense : Characterization and haematological properties

Phospholipase A 2 was isolated from Trypanosoma congolense and purified to electrophoretic homogeneity. The enzyme appeared to exist in a dimeric form with subunit molecular weights of 16 500 and 18 000. It had a pH optimum of 6·8. Kinetic analysis with different substrates, showed that the enzyme h...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Cell biochemistry and function 1993-06, Vol.11 (2), p.125-130
Hauptverfasser: Nok, Andrew J., Esievo, King A. N., Ibrahim, Sani, Ukoha, Agwu I., Ikediobi, Christopher O.
Format: Artikel
Sprache:eng
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Phospholipase A 2 was isolated from Trypanosoma congolense and purified to electrophoretic homogeneity. The enzyme appeared to exist in a dimeric form with subunit molecular weights of 16 500 and 18 000. It had a pH optimum of 6·8. Kinetic analysis with different substrates, showed that the enzyme had exceptional specificity for 1,2,dimyristoyl‐ sn ‐phosphatidylcholine and 1,2,dioleoyl‐ sn ‐phosphatidylcholine with K m values of 1·85 × 10 −3 M and 2·12 × 10 −3 M respectively. The Arrhenius plot was linear with an activation energy of 5·8 kcal mol −1 . Inhibition studies with parahydroxymercuribenzoate and tri‐butyltinoxide were positive thus implicating a thiol group at the catalytic site of the enzyme. The enzyme was stable to heat treatment and possessed haemolytic and anticoagulating properties.
ISSN:0263-6484
1099-0844
DOI:10.1002/cbf.290110208